<1> UI - 614XK-0003 DD - ISI Document Solution: 614XK AU - Rosenfeld E AU - Beauvoit B AU - Rigoulet M AU - Salmon JM MA - jmsalmon@ensam.inra.fr RA - Salmon JM TI - Non-respiratory oxygen consumption pathways in anaerobically-grown Saccharomyces cerevisiae: evidence and partial characterization SO - Yeast. 19(15):1299-1321, 2002 Nov. AS - Yeast 2002 Nov;19(15):1299-1321 PU - JOHN WILEY & SONS LTD, BAFFINS LANE CHICHESTER, W SUSSEX PO19 1UD, ENGLAND. URL: http://www.wiley.co.uk IS - 0749-503X MH - Oxygen MH - Fermentation MH - Yeast MH - Anaerobiosis. MH - Insensitive nad(p)h oxidoreductase MH - Cyanide-resistant respiration MH - Intact yeast-cells MH - Electron-transport MH - Intermediary metabolites MH - Ergosterol biosynthesis MH - Gene-expression MH - Plasma-membrane MH - Mitochondrial MH - Reductase. AB - Despite the absence of an alternative mitochondrial ubiquinol. oxidase, Saccharomyces cerevisiae consumes oxygen in an antimycin A- and cyanide-resistant manner. Cyanide-resistant respiration is typically used when the classical respiratory chain is impaired or absent (i.e in anaerobically-grown cells shifted to normoxia or in respiratory-deficient cells). We characterized the non-respiratory oxygen consumption pathways operating during anoxic-normoxic transitions in glucose-repressed resting cells. High-resolution oxygraphy confirmed that the cellular non-respiratory oxygen consumption pathway is sensitive to high concentrations of cyanide, azide, SHAM and TTFA, and revealed several new characteristics. First, the use of sterol biosynthesis inhibitors showed that this pathway makes a considerable contribution (about 25%) to both endogenous and glucose-dependent oxygen consumption. Anacrobically-grown glucose-repressed cells exhibited high apparent oxygen affinities (K-m for oxygen = 0.5-1 muM), even in mutants deficient in respiration or sterol synthesis. Exogeneously added glucose and endogenous stored carbohydrates were the only substrates that were efficient for cellular oxygen consumption (apparent K(.)mfor exogenous glucose = 2-3 mm). On the other hand, fluorimetric measurements of the cellular NAD(P)H pool showed that the cellular oxygen consumption (sterol biosynthesis and unknown pathways) was dependent more on the intracellular level of NADPH than of NADH. High oxygen affinity NADPH-dependent oxygen consumption systems were thought to be mainly localized in microsomal membranes, and several data indicated a significant contribution made by uncoupled P450 systems, together with still uncharacterized systems. Such activities are associated in vitro with a massive production of O-2(.-) and, to a lower extent, H2O2 and a likely concomitant production of H2O. Copyright (C) 2002 John Wiley Sons, Ltd. [References: 77] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Biotechnology & Applied Microbiology in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Salmon JM INRA, Lab Microbiol & Technol Fermentat, Unite Mixte Rech Sci CEnol 2 Pl Viala F-34060 Montpellier 1 France INRA, Lab Microbiol & Technol Fermentat, Unite Mixte Rech Sci CEnol F-34060 Montpellier 1 France Univ Bordeaux 2, CNRS, Inst Biochim & Genet Cellulaires F-33077 Bordeaux France <2> UI - 617FV-0020 DD - ISI Document Solution: 617FV AU - Cosper NJ AU - Eby DM AU - Kounosu A AU - Kurosawa N AU - Neidle EL AU - Kurtz DM AU - Iwasaki T AU - Scott RA MA - ncosper@uga.edu RA - Cosper NJ TI - Redox-dependent structural changes in archaeal and bacterial Rieske-type [Ne-2S] clusters SO - Protein Science. 11(12):2969-2973, 2002 Dec. AS - Protein Sci 2002 Dec;11(12):2969-2973 PU - COLD SPRING HARBOR LAB PRESS, 1 BUNGTOWN RD, PLAINVIEW, NY 11724 USA. URL: http://www.cshl.org IS - 0961-8368 MH - Anthranilate dioxygenase (antdo) MH - Archaeal rieske ferredoxin (arf) MH - Iron-sulfur cluster MH - Reduction potential MH - Rieske-type ferredoxin MH - X-ray absorption fine structure MH - X-ray absorption spectroscopy. MH - Iron-sulfur protein MH - Nuclear double-resonance MH - Forming hydrogen-bonds MH - Phthalate dioxygenase MH - 2fe-2s cluster MH - Pseudomonas-cepacia MH - Naphthalene 1,2-dioxygenase MH - Conformational-changes MH - Electron-transfer MH - Bc(1) complex. AB - Proteins containing Rieske-type [2Fe-2S] clusters play important roles in many biological electron transfer reactions. Typically, [2Fe-2S] clusters are not directly involved in the catalytic transformation of substrate, but rather supply electrons to the active site. We report herein X-ray absorption spectroscopic (XAS) data that directly demonstrate an average increase in the iron-histidine bond length of at least 0.1 Angstrom upon reduction of two distantly related Rieske-type clusters in archaeal Rieske ferredoxin from Sulfolobus solfataricus strain P-1 and bacterial anthranilate dioxygenases from Acinetobacter sp. strain ADP1. This localized redox-dependent structural change may fine tune the protein-protein interaction (in the case of ARF) or the interdomain interaction (in AntDO) to facilitate rapid electron transfer between a lower potential Rieske-type cluster and its redox partners, thereby regulating overall oxygenase reactions in the cells. [References: 31] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Cosper NJ Univ Georgia, Ctr Metalloenzyme Studies Athens, GA 30602 USA Univ Georgia, Ctr Metalloenzyme Studies Athens, GA 30602 USA Nippon Med Coll, Dept Biochem & Mol Biol, Bunkyo Ku Tokyo 1138602 Japan Soka Univ, Dept Bioengn Hachioji Tokyo 1928577 Japan <3> UI - 616NY-0021 DD - ISI Document Solution: 616NY AU - Cai SQ AU - Xu DQ MA - dqxu@iris.sipp.ac.cn RA - Xu DQ TI - Light intensity-dependent reversible down-regulation and irreversible damage of PSII in soybean leaves SO - Plant Science. 163(4):847-853, 2002 Oct. AS - Plant Sci 2002 Oct;163(4):847-853 PU - ELSEVIER SCI IRELAND LTD, CUSTOMER RELATIONS MANAGER, BAY 15, SHANNON INDUSTRIAL ESTATE CO, CLARE, IRELAND. URL: http://www.elsevier.nl IS - 0168-9452 MH - Dissociation MH - Monomerisation MH - Photodamage MH - Reversible down-regulation MH - Soybean. MH - Ii in-vivo MH - Photosystem-ii MH - Chlorophyll fluorescence MH - Reaction centers MH - Protein damage MH - Higher-plants MH - D1 protein MH - Lhc-ii MH - Photoinhibition MH - Turnover. AB - Light intensity dependence of reversible down-regulation and irreversible damage of PSII was studied by determination of chlorophyll fluorescence. PSII electron transport. D1 protein level, and oligomeric state of PSII complexes. After illumination with moderate light (700 mumol photons m(-2)s(-1), saturated for photosynthesis) for 3 h, all of the light-saturated PSII electron transport rate, D1 protein level and proportion of PSII dimer in total PSIIs in soybean leaves grown at 250-300 mumol m(-2) s(-1) had no significant change. Although PSII photochemical efficiency (Fv/Fm) declined significantly, it could recover completely after 4 h in the dark. After illumination with strong light (2000 mumol m(-2) s(-1)) for 3 h, however, the significant decreases in all parameters above were observed and Fv/Fm could not restore completely after 4 h in the dark. Moreover, the chlorophyll fluorescence parameter F685/F735 measured at 77 K dropped significantly in thylakoids from all soybean leaves illuminated at 700 (L2), 1200 (L4) and 2000 (L7) mumol m(-2) s(-1) for 3 h. After subsequent dark recovery for 3 h, F685/F735 in thylakoids from soybean leaves illuminated with L2 could recover to the level of dark control, but not in those from soybean leaves illuminated with L4 and L7. Those results indicate that the illumination with moderate light results in reversible down-regulation of some PSIIs, while illumination with strong light leads to damage of some PSIIs, namely, both reversible down-regulation and irreversible damage of PSII are light intensity-dependent. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved. [References: 34] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Xu DQ Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Plant Physiol & Ecol 300 Fenglin Rd Shanghai 200032 Peoples R China Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Plant Physiol & Ecol Shanghai 200032 Peoples R China <4> UI - 616NY-0025 DD - ISI Document Solution: 616NY AU - Merzlyak MN AU - Solovchenko AE MA - mnm@6.cellimm.bio.msu.ru RA - Merzlyak MN TI - Photostability of pigments in ripening apple fruit: a possible photoprotective role of carotenoids during plant senescence SO - Plant Science. 163(4):881-888, 2002 Oct. AS - Plant Sci 2002 Oct;163(4):881-888 PU - ELSEVIER SCI IRELAND LTD, CUSTOMER RELATIONS MANAGER, BAY 15, SHANNON INDUSTRIAL ESTATE CO, CLARE, IRELAND. URL: http://www.elsevier.nl IS - 0168-9452 MH - Apples MH - Carotenoids MH - Chlorophylls MH - Photoprotection MH - Ripening/senescence MH - Reflectance spectroscopy. MH - Leaf senescence MH - Singlet oxygen MH - Beta-carotene MH - Chlorophyll-a MH - Red-light MH - Leaves MH - Degradation MH - Plastoglobuli MH - Chloroplasts MH - Flavins. AB - Light-induced pigment destruction was studied in ripening apple (Malus domestica Borkh., cv. Antonovka) fruits with reflectance spectroscopy. The reflectance spectral changes attributable to light-induced transformation of xanthophyll cycle carotenoids (Car) preceded the pigment degradation. In green fruits, the destruction of chlorophyll and Car proceeded synchronously up to complete disappearance of both pigments. In ripening fruits with a molar chlorophyll/carotenoid ratio < 2.5-3, significant amounts of peel Car were retained at the deep stages of chlorophyll degradation. Car were especially resistant to irradiation in yellow fruits (a chlorophyll/carotenoid ratio < 0.3); the extent of their bleaching after prolonged irradiation did not exceed 20%. Irradiation of pigment solutions showed that apple fruit Car alone exhibit much higher light stability than in the presence of chlorophyll. The extent, kinetics and stoichiometry of light-induced pigment destruction in apples are consistent with the existence of two carotenoid pools, (i) closely associated with chlorophyll in chloroplast thylakoid membranes and (ii) exhibiting higher light stability localised in plastoglobuli appearing in chloroplasts undergoing transformation to gerontoplasts-chromoplast. It is suggested that the induction of carotenoid synthesis during senescence provides the protection of plastoglobuli and light-sensitive constituents of plant tissues from irradiation in the blue part of the visible spectrum. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved. [References: 38] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Merzlyak MN Moscow MV Lomonosov State Univ, Fac Biol, Dept Physiol Microorganisms GSP 2,W-234 Moscow 119992 Russia Moscow MV Lomonosov State Univ, Fac Biol, Dept Physiol Microorganisms Moscow 119992 Russia <5> UI - 616XU-0011 DD - ISI Document Solution: 616XU AU - McConnell MD AU - Koop R AU - Vasil'ev S AU - Bruce D MA - dbruce@spartan.ac.brocku.ca RA - Bruce D TI - Regulation of the distribution of chlorophyll and phycobilin-absorbed excitation energy in cyanobacteria. A structure-based model for the light state transition SO - Plant Physiology. 130(3):1201-1212, 2002 Nov. AS - Plant Physiol 2002 Nov;130(3):1201-1212 PU - AMER SOC PLANT BIOLOGISTS, 15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA. URL: http://www.aspb.org IS - 0032-0889 MH - Synechococcus sp pcc-7002 MH - Ferredoxin-nadp+ oxidoreductase MH - Respiratory electron flow MH - Ii core complexes MH - Photosystem-i MH - Thylakoid membranes MH - Crystal-structure MH - Protein-phosphorylation MH - Angstrom resolution MH - Mastigocladus-laminosus. AB - The light state transition regulates the distribution of absorbed excitation energy between the two photosystems (PSs) of photosynthesis under varying environmental conditions and/or metabolic demands. In cyanobacteria, there is evidence for the redistribution of energy absorbed by both chlorophyll (Chl) and by phycobilin pigments, and proposed mechanisms differ in the relative involvement of the two pigment types. We assayed changes in the distribution of excitation energy with 77K fluorescence emission spectroscopy determined for excitation of Chl and phycobilin pigments, in both wild-type and state transition-impaired mutant strains of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803. Action spectra for the redistribution of both Chl and phycobilin pigments were very similar in both wild-type cyanobacteria. Both state transition-impaired mutants showed no redistribution of phycobilin-absorbed excitation energy, but retained changes in Chl-absorbed excitation. Action spectra for the Chl-absorbed changes in excitation in the two mutants were similar to each other and to those observed in the two wild types. Our data show that the redistribution of excitation energy absorbed by Chl is independent of the redistribution of excitation energy absorbed by phycobilin pigments and that both changes are triggered by the same environmental light conditions. We present a model for the state transition in cyanobacteria based on the x-ray structures of PSII, PSI, and allophycocyanin consistent with these results. [References: 50] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Bruce D Brock Univ, Dept Sci Biol St Catharines ON L2S 3A1 Canada Brock Univ, Dept Sci Biol St Catharines ON L2S 3A1 Canada <6> UI - 616XU-0022 DD - ISI Document Solution: 616XU AU - Miskiewicz E AU - Ivanov AG AU - Huner NPA MA - nhuner@uwo.ca RA - Huner NPA TI - Stoichiometry of the photosynthetic apparatus and phycobilisome structure of the cyanobacterium Plectonema boryanum UTEX 485 are regulated by both light and temperature SO - Plant Physiology. 130(3):1414-1425, 2002 Nov. AS - Plant Physiol 2002 Nov;130(3):1414-1425 PU - AMER SOC PLANT BIOLOGISTS, 15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA. URL: http://www.aspb.org IS - 0032-0889 MH - Cyanophyte synechocystis pcc-6714 MH - Harvesting complex-ii MH - Sp strain pcc-6803 MH - Photosystem-i MH - Electron-transport MH - Growth irradiance MH - Chlorophyll fluorescence MH - Redox-state MH - Plastoquinone pool MH - Chlorella-vulgaris. AB - The role of growth temperature and growth irradiance on the regulation of the stoichiometry and function of the photosynthetic apparatus was examined in the cyanobacterium Plectonema boryanum UTEX 485 by comparing mid-log phase cultures grown at either 29degreesC/150 mumol m(-2) s(-1), 29degreesC/750 mumol m(-2) s(-1), 15degreesC/150 mumol m(-2) s(-1), or 15degreesC/10 mumol m(-2) s(-1). Cultures grown at 29degreesC/750 mumol m-2 s-1 were structurally and functionally similar to those grown at 15degreesC/150 mumol m(-2) s(-1), whereas cultures grown at 29degreesC/150 mumol m(-2) s(-1) were structurally and functionally similar to those grown at 15 degreesC/10 mumol m(-2) s(-1). The stoichiometry of specific components of the photosynthetic apparatus, such as the ratio of photosystem (PS) I to PSII phycobilisome size and the relative abundance of the cytochrome bb/f complex, the plastoquinone pool size, and the NAD(P)H dehydrogenase complex were regulated by both growth temperature and growth irradiance in a similar manner. This indicates that temperature and irradiance may share a common sensing/signaling pathway to regulate the stoichiometry and function of the photosynthetic apparatus in P. boryanum. In contrast, the accumulation of neither the D1 polypeptide of PSII, the large subunit of Rubisco, nor the CFl alpha-subunit appeared to be regulated by the same mechanism. Measurements of P700 photooxidation in vivo in the presence and absence of inhibitors of photosynthetic electron transport coupled with immunoblots of the NAD(P)H dehydrogenase complex in cells grown at either 29degreesC/750 mumol m(-2) s(-1) or 15degreesC/150 mumol m(-2) s(-1) are consistent with an increased flow of respiratory electrons into the photosynthetic intersystem electron transport chain maintaining P700 in a reduced state relative to cells grown at either 29degreesC/150 mumol m(-2) s(-1) or 15degreesC/10 mumol m s(-1). These results are discussed in terms of acclimation to excitation pressure imposed by either low growth temperature or high growth irradiance. [References: 50] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Huner NPA Univ Western Ontario, Dept Biol London ON N6A 5B7 Canada Univ Western Ontario, Dept Biol London ON N6A 5B7 Canada <7> UI - 616XU-0038 DD - ISI Document Solution: 616XU AU - Allakhverdiev SI AU - Nishiyama Y AU - Miyairi S AU - Yamamoto H AU - Inagaki N AU - Kanesaki Y AU - Murata N MA - murata@nibb.ac.jp RA - Murata N TI - Salt stress inhibits the repair of photodamaged photosystem II by suppressing the transcription and translation of psbA genes in Synechocystis SO - Plant Physiology. 130(3):1443-1453, 2002 Nov. AS - Plant Physiol 2002 Nov;130(3):1443-1453 PU - AMER SOC PLANT BIOLOGISTS, 15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA. URL: http://www.aspb.org IS - 0032-0889 MH - Metabolized 32-kilodalton protein MH - Terminal processing protease MH - Blue-green-algae MH - Chloroplast membranes MH - Chlamydomonas-reinhardtii MH - D1 protein MH - Photoinhibition MH - Photosynthesis MH - Light MH - Temperature. AB - Light stress and salt stress are major environmental factors that limit the efficiency of photosynthesis. However, we have found that the effects of light and salt stress on photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC 6803 are completely different. Strong light induced photodamage to PSII, whereas salt stress inhibited the repair of the photodamaged PSII and did not accelerate damage to PSII directly. The combination of light and salt stress appeared to inactivate PSII very rapidly as a consequence of their synergistic effects. Radioactive labeling of cells revealed that salt stress inhibited the synthesis of proteins de novo and, in particular, the synthesis of the D1 protein. Northern- and western-blotting analyses demonstrated that salt stress inhibited the transcription and the translation of psbA genes, which encode D1 protein. DNA microarray analysis indicated that the light-induced expression of various genes was suppressed by salt stress. Thus, our results suggest that salt stress inhibits the repair of PSII via suppression of the activities of the transcriptional and translational machinery. [References: 44] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Murata N Natl Inst Basic Biol, Dept Regulat Biol Okazaki Aichi 4448585 Japan Natl Inst Basic Biol, Dept Regulat Biol Okazaki Aichi 4448585 Japan Russian Acad Sci, Inst Basic Biol Problems Pushchino 142292 Moscow Region Russia Ehime Univ, Dept Chem Matsuyama Ehime 7908577 Japan Natl Inst Adv Ind Sci & Technol Tsukuba Ibaraki 3058566 Japan Natl Inst Agribiol Resources Tsukuba Ibaraki 3058566 Japan Grad Univ Adv Studies, Sch Life Sci, Dept Biomech Okazaki Aichi 4448585 Japan <8> UI - 616XU-0040 DD - ISI Document Solution: 616XU AU - Mewes H AU - Richter M MA - mrichter@mail.uni-mainz.de RA - Richter M TI - Supplementary ultraviolet-B radiation induces a rapid reversal of the diadinoxanthin cycle in the strong light-exposed diatom Phaeodactylum tricornutum SO - Plant Physiology. 130(3):1527-1535, 2002 Nov. AS - Plant Physiol 2002 Nov;130(3):1527-1535 PU - AMER SOC PLANT BIOLOGISTS, 15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA. URL: http://www.aspb.org IS - 0032-0889 MH - Chlorophyll-a fluorescence MH - Isolated pea thylakoids MH - Xanthophyll-cycle MH - Photosystem-ii MH - Violaxanthin cycle MH - Binding-proteins MH - Ph-dependence MH - De-epoxidase MH - Zeaxanthin MH - Algae. AB - A treatment of the diatom Phaeodactylum tricornutum with high light (HL) in the visible range led to the conversion of diadinoxanthin (Dd) to diatoxanthin (Dt). In a following treatment with HL plus supplementary ultraviolet (UV)-B, the Dt was rapidly epoxidized to Dd. Photosynthesis of the cells was inhibited under HL + UV-B. This is accounted for by direct damage by UV-B and damage because of the UV-B-induced reversal of the Dd cycle and the associated loss of photoprotection. The reversal of the Dd cycle by UV-B was faster in the presence of dithiothreitol, an inhibitor of the Dd de-epoxidase. Our results imply that the reversal of the Dd cycle by HL + UV-B was caused by an increase in the rate of gross Dt epoxidation, whereas the de-epoxidation of Dd was unaffected by UV-B. This is further supported by our finding that the in vitro de-epoxidation activity and the affinity toward the cosubstrate ascorbic acid of the Dd de-epoxidase were both unaffected by UV-B pretreatment of intact cells. We provide evidence that Dt epoxidation is normally down-regulated by a high pH gradient under HL. It is proposed that supplementary UV-B affected the pH gradient across the thylakoid membrane, which disrupted the down-regulation of Dt epoxidation and led to the observed increase in the rate of Dt epoxidation. [References: 45] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Richter M Univ Mainz, Inst Allgemeine Bot Saarstr 21 D-55099 Mainz Germany Univ Mainz, Inst Allgemeine Bot D-55099 Mainz Germany <9> UI - 616VP-0008 DD - ISI Document Solution: 616VP AU - Kada S AU - Koike H AU - Satoh K AU - Hase T AU - Fujita Y MA - fujita@nuagr1.agr.nagoya-u.ac.jp RA - Fujita Y TI - Arrest of chlorophyll synthesis and differential decrease of Photosystems I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase SO - Plant Molecular Biology. 51(2):225-235, 2002 Jan. AS - Plant Mol.Biol 2002 Jan;51(2):225-235 PU - KLUWER ACADEMIC PUBL, VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS. URL: http://www.wkap.nl IS - 0167-4412 MH - Chll gene MH - Chlorophyll synthesis MH - Cyanobacteria MH - Etiolation MH - Photosystem i MH - Photosystem ii MH - Protochlorophyllide reduction. MH - Synechocystis sp pcc-6803 MH - Increasing apoprotein stability MH - Anabaena-variabilis atcc-29413 MH - Plectonema-boryanum MH - Regulates accumulation MH - Genetic inactivation MH - Angstrom resolution MH - Barley etioplasts MH - Dark MH - Biosynthesis. AB - The chlL gene encodes one subunit of the light-independent protochlorophyllide reductase. A chIL-lacking mutant of the cyanobacterium Plectonema boryanum is unable to synthesize chlorophyll (Chl) in the dark, causing Chl synthesis to become light-dependent as in angiosperms. When the mutant cells were cultivated heterotrophic ally in the dark, Chl synthesis was arrested and the Chl content decreased exponentially in reverse profile to cell propagation, indicating that most of the pre-existing Chl was recruited for daughter cells. During this 'etiolating' process the Chl content became less than 0.5% of the original level. In parallel to this there was a decrease in the activity of Photosystem I (PSI), the amount of its core Chl-binding subunits, PsaA/PsaB, and a peripheral subunit, PsaC. Levels of transcripts for these subunits were not significantly changed upon the arrest of Chl synthesis. In contrast, Photosystem II (PSII) was maintained to a significant extent in terms of activity and protein levels of D1 and CP47 until a late stage of the etiolation, implying that PSII is newly synthesized though Chl synthesis was arrested. Low-temperature (77 K) fluorescence spectral analysis supported a selective decrease in Chl associated with PSI. Taken together, it is suggested that the pre-existing Chl molecules in periphery of PSI could be released and re-distributed for PSII biosynthesis in the etiolating cyanobacterial cells. [References: 48] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Fujita Y Nagoya Univ, Grad Sch Bioagr Sci, Lab Mol Plant Physiol Nagoya Aichi 4648601 Japan Osaka Univ, Inst Prot Res, Div Enzymol Suita Osaka 5650871 Japan Himeji Inst Technol, Fac Sci, Dept Life Sci Harima Hyogo 6781297 Japan <10> UI - 615JK-0015 DD - ISI Document Solution: 615JK AU - Johnson GA AU - Day TA MA - gj@asu.edu RA - Johnson GA TI - Enhancement of photosynthesis in Sorghum bicolor by ultraviolet radiation SO - Physiologia Plantarum. 116(4):554-562, 2002 Dec. AS - Physiol. Plant 2002 Dec;116(4):554-562 PU - BLACKWELL MUNKSGAARD, 35 NORRE SOGADE, PO BOX 2148, DK-1016 COPENHAGEN, DENMARK. URL: http://www.munksgaard.dk IS - 0031-9317 MH - Blue-green fluorescence MH - Laser-induced fluorescence MH - Beta-vulgaris l MH - Uv-b radiation MH - Action spectrum MH - Epicuticular phenolics MH - Plant-leaves MH - Ferulic acid MH - Signatures MH - Emission. AB - We assessed the influence of ultraviolet radiation (UV) on net photosynthetic CO2 assimilation rate (P-n) in Sorghum bicolor, with particular attention to examining whether UV can enhance P-n via direct absorption of UV and absorption of UV-induced blue fluorescence by photosynthetic pigments. A polychromatic UV response spectrum of leaves was constructed by measuring P-n under different UV supplements using filters that had sharp transmission cut-offs from 280 to 382 nm, against a background of non-saturating visible light. When the abaxial surface was irradiated, P-n averaged 4.6% higher with the UV supplement that cut-off UV at 311 nm, compared to lower and higher UV wavelength supplements. This former supplement differed from higher wavelength supplements by primarily providing more UV between 320 and 350 nm. To assess the possibility of direct absorption of UV by photosynthetic pigments, we measured the absorbance of extracted chlorophylls. Chlorophyll a had absorbance peaks at 340 and 389 nm that were 49 and 72% of that at the soret peak. Chlorophyll b had absorbance peaks at 315 and 346 nm that were both 35% of that at the soret peak. Since the epidermis transmits some UV, the strong UV absorbance of chlorophyll implies a potential role for irradiance beyond the bounds of the conventionally defined photosynthetically active radiation waveband (400-700 nm). To assess the role of absorption of UV-induced blue fluorescence, we measured the UV-induced fluorescence excitation and emission spectra of leaves. Abaxial excitation peaked at 328 nm, while emission peaked at 446 nm. In this analysis, we used our abaxial fluorescence excitation spectrum and the UV photosynthetic inhibition spectrum of Caldwell et al. (1986) to weight the UV irradiance with each cut-off filter, thereby estimating the potential contribution of UV-induced blue fluorescence to photosynthesis and the inhibitory effects of UV irradiance on photosynthesis, respectively. With a non-saturating visible background, we estimate that the absorption of UV-induced blue fluorescence and the direct absorption of UV by photosynthetic pigments maximally enhanced photosynthesis by about 1% each with the UV supplement that cut-off UV at 311 nm. We suggest that a portion of the incident UV on the S. bicolor leaves was used to drive photosynthesis. [References: 49] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Animal & Plant Sciences in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Johnson GA Arizona State Univ, Dept Plant Biol LSE-218,POB 871601 Tempe, AZ 85287 USA Arizona State Univ, Dept Plant Biol Tempe, AZ 85287 USA Arizona State Univ, Photosyntheses Ctr Tempe, AZ 85287 USA <11> UI - 617NX-0006 DD - ISI Document Solution: 617NX AU - Ferimazova N AU - Kupper H AU - Nedbal L AU - Trtilek M MA - hendrik.kuepper@web.de RA - Kupper H TI - New insights into photosynthetic oscillations revealed by two-dimensional microscopic measurements of chlorophyll fluorescence kinetics in intact leaves and isolated protoplasts SO - Photochemistry & Photobiology. 76(5):501-508, 2002 Nov. AS - Photochem. Photobiol 2002 Nov;76(5):501-508 PU - AMER SOC PHOTOBIOLOGY, BIOTECH PARK, 1021 15TH ST, SUITE 9, AUGUSTA, GA 30901-3158 USA. URL: http://www.kumc.edu/POL IS - 0031-8655 MH - Mathematical-model MH - Thlaspi-caerulescens MH - Glechoma-hederacea MH - A-fluorescence MH - Plant-cells MH - Assimilation MH - Chloroplasts MH - Transport MH - Cycle MH - Zinc. AB - Chlorophyll fluorescence kinetic microscopy was used to analyze photosynthetic oscillations in individual cells of leaves and in isolated leaf cell protoplasts. Four Brassicaceae species were used: Arabidopsis halleri (L.) O'Kane & Al-Shehbaz, Thlaspi fendleri (Nels.) Hitchc, Thlaspi caerulescens J.&C. Presl and Thlaspi ochroleucum Boiss et Helder. With the latter two, the measurements were extended also to isolated protoplasts. The oscillations were induced under the microscope by exposing dark-adapted samples to actinic irradiance. Detailed analysis of the induced transients revealed that they consist of several processes oscillating with different frequencies and not only one component as reported earlier. Furthermore, it was found that most of these processes are controlled inside each individual cell. This was shown by differences in oscillations in neighboring cells and protoplasts that share a uniform intercellular environment. The frequency of the dominant oscillation frequency depended neither on irradiance nor on CO2 concentration and is, therefore, not controlled by the photosynthetic rate. Characteristic differences in the frequency spectrum and damping of oscillations have been found among the plant species examined. [References: 34] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Kupper H Univ Konstanz, Fachbereich Biol, Math Nat Wissensch Sekt Postfach M665 D-78457 Constance Germany Univ Konstanz, Fachbereich Biol, Math Nat Wissensch Sekt D-78457 Constance Germany Univ S Bohemia, Fac Biol Sci Ceske Budejovice Czech Republic Univ S Bohemia, Inst Phys Biol Ceske Budejovice Czech Republic ASCR, Inst Microbiol, Dept Autotroph Microorganisms Trebon Czech Republic ASCR, Inst Landscape Ecol, Lab Appl Photobiol & Bio Imaging Nove Hardy Czech Republic Photon Syst Instruments Ltd Brno Czech Republic <12> UI - 618BC-0006 DD - ISI Document Solution: 618BC AU - Jolly RD AU - Arthur DG AU - Kay GW AU - Palmer DN MA - R.D.Jolly@massey.ac.nz RA - Jolly RD TI - Neuronal ceroid-lipofuscinosis in Borderdale sheep SO - New Zealand Veterinary Journal. 50(5):199-202, 2002 Oct. AS - N. Z. Vet. J 2002 Oct;50(5):199-202 PU - NEW ZEALAND VETERINARY ASSOC INC, PO BOX 11-212 MANNERS ST, WELLINGTON, NEW ZEALAND. URL: http://www.vets.org.nz IS - 0048-0169 MH - Sheep MH - Neuronal ceroid-lipofusinosis MH - Subunit-c MH - Mitochondrial atp synthase. MH - Mitochondrial atp synthase MH - Batten-disease MH - Ovine model MH - Subunit-c MH - Storage MH - Neurodegeneration MH - Pathogenesis MH - Protein MH - Ncl. AB - AIM: To describe the gross and histological lesions of a neurological disease in Borderdale sheep characterised clinically by blindness and circling, as a basis to its classification. METHODS: Formalin-fixed tissues were processed into paraffin wax and epoxy resin for light and electron microscopy of variously stained sections. RESULTS: Lesions were those of a lysosomal storage disease with severe neurodegeneration of the cerebral cortex. The staining reactions, autofluorescence and ultrastructure of storage material allowed the diagnosis of neuronal ceroid-lipofuscinosis associated with the accumulation of subunit-c of mitochondrial ATP synthase. CONCLUSIONS: The severity of neurodegeneration and minor differences in the ultrastructure of storage material implied that this was a different disease from other forms of ovine ceroid-lipofuscinosis that accumulate subunit-c of mitochondrial ATP synthase. An autosomal recessive mode of inheritance is considered probable. Although of only minor economic importance, this disease may be important to research into the group of ceroid-lipofuscinoses as a whole. [References: 14] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences CC - Veterinary Medicine/Animal Health in Current Contents(R)/Agricultural, Biology & Environmental Sciences. EW - 2002 week 51 IN - Reprint available from: Jolly RD Massey Univ, Inst Vet Anim & Biomed Sci Palmerston North New Zealand Massey Univ, Inst Vet Anim & Biomed Sci Palmerston North New Zealand Selwyn Rakaia Vet Serv Dunsandel 8190 New Zealand Lincoln Univ, Anim & Food Sci Div Canterbury New Zealand <13> UI - 617RA-0010 DD - ISI Document Solution: 617RA AU - Budde SMS AU - van den Heuvel LPWJ AU - Smeitink JAM MA - b.vandeheuvel@ckslkn.azn.nl RA - van den Heuvel LPWJ TI - The human complex INDUFS4 subunit: from gene structure to function and pathology SO - Mitochondrion. 2(1-2):109-115, 2002 Nov. AS - Mitochondrion 2002 Nov;2(1-2):109-115 PU - ELSEVIER SCI LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND. URL: http://www.elsevier.nl IS - 1567-7249 MH - Complex i MH - Ndufs4 MH - Leigh syndrome. MH - Dependent protein-kinase MH - Mitochondrial nadh dehydrogenase MH - Bovine heart-mitochondria MH - Beta-alanyl-nad+ MH - I deficiency MH - Leigh-syndrome MH - Aqdq subunit MH - Ndufs4 gene MH - Ubiquinone oxidoreductase MH - Oxidative-phosphorylation. AB - Complex I is the first and largest enzyme of the oxidative phosphorylation system. It consists of at least 43 subunits. Recent studies have shown that the NDUFS4 subunit of complex I contributes to the activation of the complex through cAMP dependent phosphorylation of a conserved site (RVS) located at the C-terminal region of this protein. This report focuses on the NDUFS4 subunit. Summarized is the current knowledge of this subunit, from gene structure to function and pathology. (C) 2002 Elsevier Science B.V. and Mitochondria Research Society. All rights reserved. [References: 34] LG - English PT - Article SB - Current Contents(R)/Clinical Medicine CC - Research/Laboratory Medicine & Medical Technology in Current Contents(R)/Clinical Medicine. EW - 2002 week 51 IN - Reprint available from: van den Heuvel LPWJ Univ Nijmegen, Ctr Med, Dept Paediat, Nijmegen Ctr Mitochondrial Disorders Geert Grooteplein 20,POB 9101 NL-6500 HB Nijmegen Netherlands Univ Nijmegen, Ctr Med, Dept Paediat, Nijmegen Ctr Mitochondrial Disorders NL-6500 HB Nijmegen Netherlands <14> UI - 615ZD-0005 DD - ISI Document Solution: 615ZD AU - Hanley PJ AU - Ray J AU - Brandt U AU - Daut J MA - daut@mailer.uni-marburg.de RA - Daut J TI - Halothane, isoflurane and sevoflurane inhibit NADH : ubiquinone oxidoreductase (complex I) of cardiac mitochondria SO - Journal of Physiology-London. 544(3):687-693, 2002 Nov 1. AS - J. Physiol.-London 2002 Nov 1;544(3):687-693 PU - CAMBRIDGE UNIV PRESS, 40 WEST 20TH ST, NEW YORK, NY 10011-4221 USA. URL: http://www.cup.org IS - 0022-3751 MH - Rat ventricular myocytes MH - Anesthetic nitrous-oxide MH - Bovine heart MH - General-anesthetics MH - Energy-expenditure MH - Mechanisms MH - Muscle MH - Induction MH - Particles MH - Children. AB - We have investigated the effects of volatile anaesthetics on electron transport chain activity in the mammalian heart. Halothane, isoflurane and sevoflurane reversibly increased NADH fluorescence (autofluorescence) in intact ventricular myocytes of guinea-pig, suggesting that NADH oxidation was impaired. Using pig heart submitochondrial particles we found that the anaesthetics; dose-dependently inhibited NADH oxidation in the order: halothane > isoflurane = sevoflurane. Succinate oxidation was unaffected by either isoflurane or sevoflurane, indicating that these agents selectively inhibit complex I (NADH:ubiquinone oxidoreductase). In addition to inhibiting NADH oxidation, halothane also inhibited succinate oxidation (and succinate dehydrogenase), albeit to a lesser extent. To test the hypothesis that complex I is a target of volatile anaesthetics, we examined the effects of these agents on NADH:ubiquinone oxidoreductase (EC 1.6.99.3) activity using the ubiquinone analogue DBQ (decylubiquinone) as substrate. Halothane, isoflurane and sevoflurane dose-dependently inhibited NADH:DBQ oxidoreductase activity. Unlike the classical inhibitor rotenone, none of the anaesthetics completely inhibited enzyme activity at high concentration, suggesting that these agents bind weakly to the 'hydrophobic inhibitory site' of complex 1. In conclusion, halothane, isoflurane and sevoflurane inhibit complex I (NADH:ubiquinone oxidoreductase) of the electron transport chain. At concentrations of similar to2 MAC (minimal alveolar concentration), the activity of NADH:ubiquinone oxidoreductase was reduced by about 20% in the presence of halothane or isoflurane, and by about 10% in the presence of sevoflurane. These inhibitory effects are unlikely to compromise cardiac performance at usual clinical concentrations, but may contribute to the mechanism by which volatile anaesthetics induce pharmacological preconditioning. [References: 40] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Physiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Daut J Univ Marburg, Inst Physiol Deutschhausstr 2 D-35037 Marburg Germany Univ Frankfurt Klinikum, Inst Biochem 1 D-60590 Frankfurt Germany Univ Marburg, Inst Normale & Pathol Physiol D-35037 Marburg Germany <15> UI - 614GR-0022 DD - ISI Document Solution: 614GR AU - Johnson ET AU - Muh F AU - Nabedryk E AU - Williams JC AU - Allen JP AU - Lubitz W AU - Breton J AU - Parson WW RA - Parson WW TI - Electronic and vibronic coupling of the special pair of bacteriochlorophylls in photosynthetic reaction centers from wild-type and mutant strains of Rhodobacter sphaeroides SO - Journal of Physical Chemistry B. 106(45):11859-11869, 2002 Nov 14. AS - J. Phys. Chem. B 2002 Nov 14;106(45):11859-11869 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 1520-6106 MH - Bacterial reaction centers MH - Induced structural-changes MH - Ftir difference spectroscopy MH - Viridis reaction centers MH - Rhodopseudomonas-viridis MH - Primary donor MH - Charge-separation MH - Transfer kinetics MH - Triple-resonance MH - Radical cations. AB - The photosynthetic reaction center (RC) is an integral membrane protein that carries out the initial charge-separation reactions of photosynthesis. Upon light excitation, a pair (P) of bacteriochlorophylls (Bchls) donates an electron to a bacteriopheophytin (H-L), generating an ion-pair state (P+HL-). Previous ENDOR studies of RCs from the purple bacterium Rhodobacter sphaeroides have shown that the unpaired electron of P+ is distributed unequally between the two Bchls of P, with about 2/3 of the unpaired spin and positive charge residing on the Bchl bound to subunit L (P-L) and 1/3 on the Bchl bound to M (P-M). To investigate the protein's role in establishing the energies of the cations P-L(+) and P-M(+) through long-range electrostatic interactions, we mutated Arg L135 and Arg M164 individually to Leu or Glu and measured the effects on the Special TRIPLE and FTIR spectra of P+. These highly conserved residues occupy homologous positions on either side of P but have no hydrogen bonds or steric interactions with the pigments. Previous work has shown that replacing Arg by Leu at either site lowers the midpoint potential (E-m) of P/P+ by about 15 mV; replacing it by Glu lowers the E-m by about 35 mV. We found that the mutations also alter the spin distribution in P+. The mutation R(L135)E stabilizes P-L(+) relative to P-M(+), increasing the ratio of the spins to 3.1, whereas R(M164)E decreases the spin ratio to 1.3. Replacing R(L135) or R(M164) by Leu gave spin ratios of 2.9 or 1.6, respectively. FTIR measurements showed that the mutations also affect the vibrational spectra of P and P+ and the electronic transition between the eigenstates of P+. The R(L135)E mutation increases the splitting between the keto C=O stretching bands of P-L(+) and P-M(+), whereas the R(M164)E mutation decreases this splitting. The changes in the keto frequency are correlated with calculated changes in the projection of the local electric field along the C=O bond, and give a Stark tuning rate in the range 0.81-1.45 cm(-1)/(MV/cm). Cooling the RCs to 100 K during illumination increases the splitting between the keto bands of P-L(+) and P-M(+) in wild-type and R(L135)E RCs and shifts the electronic transition to higher energies, suggesting that relaxations of the protein further stabilize P-L(+) relative to P-M(+). Fitting the electrochemical, ENDOR, and FTIR data to a self-consistent molecular orbital model required including both vibronic and electronic coupling of P-L(+) and P-M(+) and yielded an electronic coupling constant of approximately -155 meV and a reorganization energy of approximately 220 meV. [References: 87] LG - English PT - Article SB - Current Contents(R)/Physical, Chemical & Earth Sciences CC - Physical Chemistry/Chemical Physics in Current Contents(R)/Physical, Chemical & Earth Sciences. EW - 2002 week 51 IN - Reprint available from: Parson WW Univ Washington, Dept Biochem Box 357350 Seattle, WA 98195 USA Univ Washington, Dept Biochem Seattle, WA 98195 USA Free Univ Berlin, Inst Expt Phys D-14195 Berlin Germany CEA Saclay, Serv Bioenerget F-91191 Gif Sur Yvette France Arizona State Univ, Dept Chem & Biochem Tempe, AZ 85287 USA Max Planck Inst Strahlenchem D-45470 Mulheim Germany <16> UI - 617AD-0012 DD - ISI Document Solution: 617AD AU - Jeong DH AU - Jang SM AU - Hwang IW AU - Kim D AU - Yoshida N AU - Osuka A RA - Osuka A TI - Investigation of interporphyrin charge resonance of dihedral angle controlled porphyrin dimers by resonance Raman spectroscopy and MO approaches SO - Journal of Physical Chemistry. 106(46):11054-11063, 2002 Nov 21. AS - J. Phys. Chem. A 2002 Nov 21;106(46):11054-11063 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 1089-5639 MH - Photosynthetic reaction-center MH - Photoinduced electron-transfer MH - Sandwich complexes MH - Hybrid diporphyrins MH - Excitation-energy MH - Optical control MH - Building-block MH - Bridges MH - Arrays MH - Models. AB - Strongly interacting porphyrin dimers as a form of cofacial or side-to-side linkage have been ideally suited for investigation on the structure-electronic property relationship in porphyrin dimers. The relative orientation and interchromophore distance determined by the dihedral angle between the two porphyrin units are key factors in controlling the interchromophoric interaction. In the present work, directly linked porphyrin dimers with a systematic change in the dihedral angle between the two porphyrin planes have been investigated by resonance Raman (RR) and emission spectroscopies. Extremely strong molecular orbital interactions between the porphyrin units by decreasing the dihedral angle give rise to strongly enhanced interporphyrin charge-resonance transitions. With a decrease of the dihedral angle, unique RR spectra of the porphyrin dimers were also observed depending on the excitation wavelengths of 406.7, 457.9, and 488.0 nm. With the aid of supermolecular MO approaches it was found that the charge-resonance band at ca. 450 nm involves a(1u)(A) --> (1/root2)(e(gx)+e(gy))(B) transition. Upon excitation at this transition, the Raman modes involving nu(CalphaCbeta) and nu(CalphaCbeta) motions such as nu(38), nu(11), and nu(3) are predominantly enhanced. The MO calculation also revealed a considerable mixing between the charge-resonance transition and the excitonic transition with a decrease of the dihedral angle. The fast component in the fluorescence decay (ca. 500 ps) was found to increase in. its contribution as the dihedral angle decreases, which was tentatively interpreted in terms of the vibronic mixing of the Q-band mixed with the charge-resonance transition. [References: 65] LG - English PT - Article SB - Current Contents(R)/Physical, Chemical & Earth Sciences CC - Physical Chemistry/Chemical Physics in Current Contents(R)/Physical, Chemical & Earth Sciences. EW - 2002 week 51 IN - Reprint available from: Osuka A Yonsei Univ, Ctr Ultrafast Opt Characterist Control Seoul 120749 South Korea Yonsei Univ, Ctr Ultrafast Opt Characterist Control Seoul 120749 South Korea Yonsei Univ, Dept Chem Seoul 120749 South Korea Kyoto Univ, Grad Sch Sci, Dept Chem Kyoto 6068502 Japan <17> UI - 617TC-0008 DD - ISI Document Solution: 617TC AU - Oldham KM AU - Wise SR AU - Chen L AU - Stacewicz-Sapuntzakis M AU - Burns J AU - Bowen PE MA - koldham@protocare.com RA - Oldham KM TI - A longitudinal evaluation of oxidative stress in trauma patients SO - Jpen: Journal of Parenteral & Enteral Nutrition. 26(3):189-197, 2002 May-Jun. AS - J. Parenter. Enter. Nutr 2002 May-Jun;26(3):189-197 PU - AMER SOC PARENTERAL & ENTERAL NUTRITION, 8630 FENTON STREET SUITE 412, SILVER SPRING, MD 20910 USA. URL: http://www.clinnutr.org IS - 0148-6071 MH - Respiratory-distress-syndrome MH - Alpha-tocopherol MH - Antioxidant vitamins MH - Lipid-peroxidation MH - Xanthine-oxidase MH - Organ failure MH - Dna-damage MH - Sepsis MH - 8-hydroxydeoxyguanosine MH - Carotenoids. AB - Background: The purpose of this study was to determine the course of oxidative stress in trauma patients as measured by antioxidant disappearance and modulation of DNA damage. The study also explored the role of injury severity and the effect of changes in plasma lipoprotein concentration as the result of hemodilution on lipid-soluble plasma antioxidant concentrations. Methods: The study population included 17 adult male trauma patients in an urban level-1 trauma hospital and 12 healthy adult male controls. Blood was collected immediately after admission in the emergency room, and on days 2, 3, 4, 6, and 8 of admission. Plasma antioxidant concentrations and total cholesterol concentrations were evaluated. DNA damage was evaluated using the ratio of 8-hydroxydeoxyguanosine to deoxyguanosine (8OhdG to dG). Admission data were compared with data from controls. Results: Plasma antioxidant concentrations (except alpha-tocopherol) significantly decreased by 9.9% to 34.3% in the 24 hours after trauma and remained depressed throughout day 8. Repeated measures regression analysis for trend showed a significant increase in unadjusted alpha-tocopherol from day 1 to day 8 (P <.008). No other unadjusted antioxidant or plasma cholesterol showed a significant change. After individually adjusting antioxidant concentrations by total cholesterol, only gamma-tocopherol (22.2%) and lycopene (22.6%) were decreased (p <.04) in the 24 hours after trauma. Repeated measures regression analysis for trend for the cholesterol-adjusted antioxidants showed a significant decrease from day 1 to day 8 for cholesterol-adjusted alpha-carotene (p <.007) and P-carotene (p <.007). Trauma patients were divided into more and less severely injured groups based on Injury Severity Score (ISS). Decreases in antioxidant concentration from day 1 to day 2 were found for the patients in the more injured group, with no significant differences from day 1 to day 2 in the less severely injured group. Cholesterol-adjusted gamma-tocopherol (29.7%, p <.003) and lycopene (32.7%, p <.05) decreased from day 1 to day 2 in the more severely injured group. Using repeated measures regression analysis for trend, the only antioxidant that was significantly different in the high versus low ISS groups from day 1 through day 6 was cholesterol-adjusted lutein-zeaxanthin (p <.02). Compared with controls, trauma patients had significantly lower (27.3% to 64.9%) concentrations of all cholesterol-adjusted antioxidants at day 1 except for lycopene. Trauma patients had higher leukocyte 8OhdG to dG ratios at admission (42.6%, p <.05), but 8OhdG to dG ratios tended to decrease over the 24 hours after trauma (P <.07). This decrease was greater in the 3 trauma patients with an admission 8OhdG to dG ratio greater than 6 X 10(-5) (59.3% versus 0.05%, p <.03). Conclusions: The difference in antioxidant concentrations between trauma patients and controls may have been associated with oxidative stress or with a poorer diet. The difference between antioxidant concentrations and cholesterol-adjusted antioxidant concentrations is likely caused by hemodilution or by changes in plasma lipid levels as a result of trauma. Therefore, individually adjusting lipid-soluble antioxidant concentrations by total cholesterol concentrations is important in trauma patients. Leukocyte 8ohdG to dG ratios were already elevated in trauma patients on admission but returned nearly to control levels 24 hours later, indicating short-term responsiveness to DNA oxidation in trauma patients and an extensive capacity for DNA repair within 24 hours. [References: 43] LG - English PT - Article SB - Current Contents(R)/Clinical Medicine CC - Endocrinology, Metabolism & Nutrition in Current Contents(R)/Clinical Medicine. EW - 2002 week 51 IN - Reprint available from: Oldham KM Univ Illinois, Dept Human Nutr & Dietet M-C 517,1919 W Taylor St Chicago, IL 60612 USA Univ Illinois, Dept Human Nutr & Dietet Chicago, IL 60612 USA Mt Sinai Hosp Med Ctr, Dept Nutr & Food Sci Chicago, IL USA Finch Univ Hlth Sci Chicago Med Sch, Dept Surg Chicago, IL USA Univ Illinois, Hlth Res Ctr Chicago, IL 60612 USA Univ Illinois, Policy Ctr Chicago, IL 60612 USA <18> UI - 615PA-0009 DD - ISI Document Solution: 615PA AU - Apt KE AU - Zaslavkaia L AU - Lippmeier JC AU - Lang M AU - Kilian O AU - Wetherbee R AU - Grossman AR AU - Kroth PG MA - kirkapt@martekbio.com, peter.kroth@uni-konstanz.de RA - Apt KE TI - In vivo characterization of diatom multipartite plastid targeting signals SO - Journal of Cell Science. 115(21):4061-4069, 2002 Nov 1. AS - J. Cell Sci 2002 Nov 1;115(21):4061-4069 PU - COMPANY OF BIOLOGISTS LTD, BIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND. URL: http://www.cityscape.co.uk/users/ag64/ IS - 0021-9533 MH - Complex plastids MH - Bipartite pre-sequence MH - Diatom MH - Green MH - Fluorescent protein MH - Plastid import. MH - Light-harvesting proteins MH - Phaeodactylum-tricornutum MH - Endoplasmic-reticulum MH - Gene-transfer MH - Chloroplasts MH - Transport MH - Evolution MH - Complex MH - Import MH - Algae. AB - Plastids of diatoms and related algae are delineated by four membranes: the outermost membrane (CER) is continuous with the endoplasmic reticulum while the inner two membranes are homologous to plastid envelope membranes of vascular plants and green algae. Proteins are transported into these plastids by pre-sequences that have two recognizable domains. To characterize targeting of polypeptides within diatom cells, we generated constructs encoding green fluorecent protein (GFP) fused to leader sequences. A fusion of GFP to the pre-sequence of BiP [an endoplasmic reticulum (ER)-localized chaperone] resulted in accumulation of GFP within the ER; a construct encoding the pre-sequence of a plastid protein fused to GFP was directed into the plastids. Additional constructs demonstrated that the N-terminal region of the bipartite plastid targeting pre-sequence was necessary for transport of polypeptides to the lumen of the ER, while the C-terminal region was shown to enable the proteins to traverse the plastid double envelope membrane. Our data strongly. support the hypothesis of a multi-step plastid targeting process in chromophytic algae and raises questions about the continuity of the ER and CER and the function of the latter in polypeptide trafficking. [References: 47] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Cell & Developmental Biology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Apt KE Martek Biosci Corp 6480 Dobbin Rd Columbia, MD 21045 USA Martek Biosci Corp Columbia, MD 21045 USA Univ Konstanz, Fachbereich Biol D-78457 Constance Germany Univ Melbourne, Sch Bot Parkville Vic 3052 Australia Carnegie Inst Washington, Dept Plant Biol Stanford, CA 94305 USA <19> UI - 615XE-0003 DD - ISI Document Solution: 615XE AU - Zhang M AU - Mileykovskaya E AU - Dowhan W MA - William.Dowhan@uth.tmc.edu RA - Dowhan W TI - Gluing the respiratory chain together - Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane SO - Journal of Biological Chemistry. 277(46):43553-43556, 2002 Nov 15. AS - J. Biol. Chem 2002 Nov 15;277(46):43553-43556 PU - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA. URL: http://www.asbmb.org IS - 0021-9258 MH - Cytochrome bc(1) complex MH - Saccharomyces-cerevisiae MH - Acridine-orange MH - Yeast MH - Protein MH - System MH - Phospholipids MH - Digestion MH - Synthase MH - Vectors. AB - Cytochrome bc(1) complex (complex III) and cytochrome c oxidase complex (complex IV) are multisubunit homodimers that are essential components of the mitochondrial respiratory chain. Complexes III and IV associate to form a supercomplex that can be displayed using blue native polyacrylamide gel electrophoresis. Both homodimeric complexes contain tightly associated cardiolipin (CL) required for function. We report here that in a crd1Delta strain of yeast (null in expression of CL synthase) similar to90% of complexes III and IV were observed as individual homodimers; only the supercomplex was observed with CRD1 wild type cells. Introduction of a plasmid born copy of the CRD1 gene under exogenous regulation by doxycycline made possible controlled variation in the in vivo CL levels. At an intermediate level of CL, a mixture of individual homodimers (30%) and supercomplex (70%) was observed. These results strongly indicate that CL plays a central role in higher order organization of components of the respiratory chain of mitochondria. [References: 25] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Dowhan W Univ Texas, Sch Med, Dept Biochem & Mol Biol POB 20708 Houston, TX 77225 USA Univ Texas, Sch Med, Dept Biochem & Mol Biol Houston, TX 77225 USA <20> UI - 615XE-0014 DD - ISI Document Solution: 615XE AU - Kolodziejczak M AU - Kolaczkowska A AU - Szczesny B AU - Urantowka A AU - Knorpp C AU - Kieleczawa J AU - Janska H MA - Janska@bf.uni.wroc.pl RA - Janska H TI - A higher plant mitochondrial homologue of the yeast m-AAA protease - Molecular cloning, localization, and putative function SO - Journal of Biological Chemistry. 277(46):43792-43798, 2002 Nov 15. AS - J. Biol. Chem 2002 Nov 15;277(46):43792-43798 PU - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA. URL: http://www.asbmb.org IS - 0021-9258 MH - Chaperone-like activity MH - Inner membrane MH - Saccharomyces-cerevisiae MH - Ftsh protease MH - Proteins MH - Chloroplast MH - Degradation MH - Mutations MH - Metalloprotease MH - Arabidopsis. AB - Mitochondrial AAA metalloproteases play a fundamental role in mitochondrial biogenesis and function. They have been identified in yeast and animals but not yet in plants. This work describes the isolation and sequence analysis of the full-length cDNA from the pea (Pisum sativum) with significant homology to the yeast matrix AAA (m-AAA) protease. The product of this clone was imported into isolated pea mitochondria where it was processed to its mature form (PsFtsH). We have shown that the central region of PsFtsH containing the chaperone domain is exposed to the matrix space. Furthermore, we have demonstrated that the pea protease can complement respiration deficiency in the yta10 and/or yta12 null yeast mutants, indicating that the plant protein can compensate for the loss of at least some of the important m-AAA functions in yeast. Based on biochemical experiments using isolated pea mitochondria, we propose that PsFtsH-like m-AAA is involved in the accumulation of the subunit 9 of the ATP synthase in the mitochondrial membrane. [References: 31] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Janska H Wroclaw B Beirut Univ, Inst Biochem & Mol Biol Tamka 2 PL-50137 Wroclaw Poland Wroclaw B Beirut Univ, Inst Biochem & Mol Biol PL-50137 Wroclaw Poland Swedish Univ Agr Sci, Dept Plant Biol S-75007 Uppsala Sweden Brookhaven Natl Lab, Dept Biol Upton, NY 11973 USA <21> UI - 615XE-0054 DD - ISI Document Solution: 615XE AU - Berthold DA AU - Voevodskaya N AU - Stenmark P AU - Graslund A AU - Nordlund P MA - berthold@dbb.su.se RA - Berthold DA TI - EPR studies of the mitochondrial alternative oxidase - Evidence for a diiron carboxylate center SO - Journal of Biological Chemistry. 277(46):43608-43614, 2002 Nov 15. AS - J. Biol. Chem 2002 Nov 15;277(46):43608-43614 PU - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA. URL: http://www.asbmb.org IS - 0021-9258 MH - Higher-plant-mitochondria MH - Arum-maculatum mitochondria MH - Methylosinus-trichosporium ob3b MH - Cyanide-resistant respiration MH - Binuclear iron center MH - Herpes-simplex virus MH - Methane monooxygenase MH - Partial-purification MH - Ribonucleotide reductase MH - Active-site. AB - The alternative oxidase (AOX) is a ubiquinol oxidase found in the mitochondrial respiratory chain of plants as well as some fungi and protists. It has been predicted to contain a coupled diiron center on the basis of a conserved sequence motif consisting of the proposed iron ligands, four glutamate and two histidine residues. However, this prediction has not been experimentally verified. Here we report the high level expression of the Arabidopsis thaliana alternative oxidase AOX1a as a maltose-binding protein fusion in Escherichia coli. Reduction and reoxidation of a sample of isolated E. coli membranes containing the alternative oxidase generated an EPR signal characteristic of a mixed-valent Fe(II)/Fe(III) binuclear iron center. The high anisotropy of the signal, the low value of the g-average tensor, and a small exchange coupling (-J) suggest that the iron center is hydroxo-bridged. A reduced membrane preparation yielded a parallel mode EPR signal with a g-value of about 15. In AOX containing a mutation of a putative glutamate ligand of the diiron center (E222A or E273A) the EPR signals are absent. These data provide evidence for an antiferromagnetic-coupled binuclear iron center, and together with the conserved sequence motif, identify the alternative oxidase as belonging to the growing family of diiron carboxylate proteins. The alternative oxidase is the first integral membrane protein in this family, and adds a new catalytic activity (ubiquinol oxidation) to this group of enzymatically diverse proteins. [References: 55] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Berthold DA Stockholm Univ, Dept Biochem & Biophys Svante Arrhenius Vag 12 S-10691 Stockholm Sweden Stockholm Univ, Dept Biochem & Biophys S-10691 Stockholm Sweden <22> UI - 615JT-0018 DD - ISI Document Solution: 615JT AU - Schaefer AL AU - Taylor TA AU - Beatty JT AU - Greenberg EP MA - everettgreenberg@uiowa.edu RA - Greenberg EP TI - Long-chain acyl-homoserine lactone quorum-sensing regulation of Rhodobacter capsulatus gene transfer agent production SO - Journal of Bacteriology. 184(23):6515-6521, 2002 Dec. AS - J. Bacteriol 2002 Dec;184(23):6515-6521 PU - AMER SOC MICROBIOLOGY, 1752 N ST NW, WASHINGTON, DC 20036-2904 USA. URL: http://www.asmusa.org IS - 0021-9193 MH - Vibrio-fischeri luminescence MH - Aeruginosa virulence genes MH - Gram-negative bacteria MH - Pseudomonas-aeruginosa MH - Rhodopseudomonas-capsulata MH - Photobacterium-fischeri MH - Luxr protein MH - Autoinducer MH - Identification MH - Signals. AB - Many proteobacteria use acyl-homoserine lactones as quorum-sensing signals. Traditionally, biological detection systems have been used to identify bacteria that produce acyl-homoserine lactones, although the specificities of these detection systems can limit discovery. We used a sensitive approach that did not require a bioassay to detect production of long-acyl-chain homoserine lactone production by Rhodobacter capsulatus and Paracoccus denitrificans. These long-chain acyl-homoserine lactones are not readily detected by standard bioassays. The most abundant acyl-homoserine lactone was N-hexadecanoyl-homoserine lactone. The long-chain acyl-homoserine lactones were concentrated in cells but were also found in the culture fluid. An R. capsulatus gene responsible for long-chain acyl-homoserine lactone synthesis was identified. A mutation in this gene, which we named gtaI, resulted in decreased production of the R. capsulatus gene transfer agent, and gene transfer agent production was restored by exogenous addition of N-hexadecanoyl-homoserine lactone. Thus, long-chain acyl-homoserine lactones serve as quorum-sensing signals to enhance genetic exchange in R. capsulatus. [References: 49] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Greenberg EP Univ Iowa, Dept Microbiol 540 EMRB,Newton Rd Iowa City, IA 52242 USA Univ Iowa, Dept Microbiol Iowa City, IA 52242 USA Univ Iowa, WM Keck Fdn, Microbial Communities & Cell Signaling Lab Iowa City, IA 52242 USA Univ British Columbia, Dept Microbiol & Immunol Vancouver BC V6T 1Z3 Canada <23> UI - 615JT-0034 DD - ISI Document Solution: 615JT AU - Cheng QM AU - Park JT MA - James.Park@tufts.edu RA - Park JT TI - Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides SO - Journal of Bacteriology. 184(23):6434-6436, 2002 Dec. AS - J. Bacteriol 2002 Dec;184(23):6434-6436 PU - AMER SOC MICROBIOLOGY, 1752 N ST NW, WASHINGTON, DC 20036-2904 USA. URL: http://www.asmusa.org IS - 0021-9193 MH - Beta-lactamase induction MH - L-alanine amidase MH - N-acetylglucosaminidase MH - Escherichia-coli MH - Enterobacter-cloacae. AB - AmpG was originally identified as a gene required for induction of beta-lactamase. Subsequently, we found AmpG to be a permease required for recycling of murein tripeptide and uptake of anhydro-muropeptides. We have now studied the specificity of the AmpG permease. The principal requirement is for the presence of the disaccharide, N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc). These unique substrates for AmpG, which contain murein peptides linked to GlcNAc-anhMurNAc, are produced by turnover of the cell wall during logarithmic growth. AmpG permease is sensitive to carbonylcyanide m-chlorophenylhydrazone, demonstrating that AmpG permease is a single-component permease and that transport is dependent on the proton motive force. [References: 13] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Park JT Tufts Univ, Sch Med, Dept Mol Biol & Microbiol 136 Harrison Ave Boston, MA 02111 USA Tufts Univ, Sch Med, Dept Mol Biol & Microbiol Boston, MA 02111 USA <24> UI - 615JT-0038 DD - ISI Document Solution: 615JT AU - Gibson JL AU - Dubbs JA AU - Tabita FR MA - tabita.1@osu.edu RA - Tabita FR TI - Differential expression of the CO2 fixation operons of Rhodobacter sphaeroides by the Prr/Reg two-component system during chemoautotrophic growth SO - Journal of Bacteriology. 184(23):6654-6664, 2002 Dec. AS - J. Bacteriol 2002 Dec;184(23):6654-6664 PU - AMER SOC MICROBIOLOGY, 1752 N ST NW, WASHINGTON, DC 20036-2904 USA. URL: http://www.asmusa.org IS - 0021-9193 MH - Photosynthesis gene-expression MH - Bisphosphate carboxylase-oxygenase MH - Signal-transduction system MH - Rhodopseudomonas-sphaeroides MH - Nucleotide-sequence MH - Histidine kinase MH - Form-i MH - Rhodobacter-sphaeroides-2.4.1 MH - Capsulatus MH - Mutant. AB - In Rhodobacter sphaeroides, the two ebb operons encoding duplicated Calvin-Benson Bassham (CBB) CO2 fixation reductive pentose phosphate cycle structural genes are differentially controlled. In attempts to define the molecular basis for the differential regulation, the effects of mutations in genes encoding a subunit of Cbb3 cytochrome oxidase, ccoP, and a global response regulator, prrA (regA), were characterized with respect to CO2 fixation (ebb) gene expression by using translational lac fusions to the R. sphaeroides cbb, and cbb, promoters. Inactivation of the ccoP gene resulted in derepression of both promoters during chemoheterotophic growth, where ebb expression is normally repressed; expression was also enhanced over normal levels during phototrophic growth. The prrA mutation effected reduced expression of ebb, and cbb, promoters during chemoheterotrophic growth, whereas intermediate levels of expression were observed in a double ccoP prrA mutant. PrrA and ccoP1 prrA strains cannot grow phototrophically, so it is impossible to examine ebb expression in these backgrounds under this growth mode. In this study, however, we found that PrrA mutants of R. sphaeraides were capable of chemoautotrophic growth, allowing, for the first time, an opportunity to directly examine the requirement of PrrA for ebb gene expression in vivo under growth conditions where the CBB cycle and CO2 fixation are required. Expression from the cbb, promoter was severely reduced in the PrrA mutants during chemoautotrophic growth, whereas cbb, expression was either unaffected or enhanced. Mutations in ccoQ had no effect on expression from either promoter. These observations suggest that the Prr signal transduction pathway is not always directly linked to Cbb3 cytochrome oxidase activity, at least with respect to ebb gene expression. In addition, lac fusions containing various lengths of the cbb, promoter demonstrated distinct sequences involved in positive regulation during photoautotrophic versus chemoautotrophic growth, suggesting that different regulatory proteins may be involved. In Rhodobacter capsulatus, ribulose 1,5-bis phosphate carboxylase-oxygenase (RubisCO) expression was not affected by cco mutations during photoheterotrophic growth, suggesting that differences exist in signal transduction pathways regulating cbb genes in the related organisms. [References: 35] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Tabita FR Ohio State Univ, Dept Microbiol 484 W 12Th Ave Columbus, OH 43210 USA Ohio State Univ, Dept Microbiol Columbus, OH 43210 USA Ohio State Univ, Plant Mol Biol Biotechnol Program Columbus, OH 43210 USA <25> UI - 615JT-0039 DD - ISI Document Solution: 615JT AU - Smith SA AU - Tabita FR MA - tabita.1@osu.edu RA - Tabita FR TI - Up-regulated expression of the cbb(I) and cbb(II) operons during photoheterotrophic growth of a ribulose 1,5-bisphosphate carboxylase-oxygenase deletion mutant of Rhodobacter sphaeroides SO - Journal of Bacteriology. 184(23):6721-6724, 2002 Dec. AS - J. Bacteriol 2002 Dec;184(23):6721-6724 PU - AMER SOC MICROBIOLOGY, 1752 N ST NW, WASHINGTON, DC 20036-2904 USA. URL: http://www.asmusa.org IS - 0021-9193 MH - Signal-transduction system MH - Co2 fixation operon MH - Form-i MH - Gene-expression MH - Rhodopseudomonas-sphaeroides MH - Nucleotide-sequence MH - Calvin cycle MH - Phosphoribulokinase MH - Photosynthesis MH - Mutagenesis. AB - In a Rhodobacter sphaeroides ribulose 1,5-bisphosphate carboxylase-oxygenase deletion strain that requires an exogenous electron donor for photoheterotrophic growth, transcription of the genes of the Calvin-Benson-Bassham (CBB) cycle was increased. This finding pointed to a potential physiological effector that enhances the capability of the positive transcriptional activator CbbR to mediate ebb transcription. This effector is most likely ribulose 1,5-bisphosphate or a metabolite derived from this CBB pathway intermediate. [References: 25] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Tabita FR Ohio State Univ, Dept Microbiol 484 W 12Th Ave Columbus, OH 43210 USA Ohio State Univ, Dept Microbiol Columbus, OH 43210 USA Ohio State Univ, Plant Mol Biol & Biotechnol Program Columbus, OH 43210 USA <26> UI - 615JT-0041 DD - ISI Document Solution: 615JT AU - Herdendorf TJ AU - McCaslin DR AU - Forest KT MA - forest@bact.wisc.edu RA - Forest KT TI - Aquifex aeolicus PilT, homologue of a surface motility protein, is a thermostable oligomeric NTPase SO - Journal of Bacteriology. 184(23):6465-6471, 2002 Dec. AS - J. Bacteriol 2002 Dec;184(23):6465-6471 PU - AMER SOC MICROBIOLOGY, 1752 N ST NW, WASHINGTON, DC 20036-2904 USA. URL: http://www.asmusa.org IS - 0021-9193 MH - Cag pathogenicity island MH - Twitching motility MH - Iv pilus MH - Neisseria-gonorrhoeae MH - Myxococcus-xanthus MH - Natural transformation MH - Gliding motility MH - Atp synthase MH - Gene MH - Biogenesis. AB - Bacterial surface motility works by retraction of surface-attached type IV pili. This retraction requires the PilT protein, a member of a large family of putative NTPases from type 11 and IV secretion systems. In this study, the PilT homologue from the thermophilic eubacterium Aquifex aeolicus was cloned, overexpressed, and purified. A. aeolicus PilT was shown to be a thermostable ATPase with a specific activity of 15.7 nmol of ATP hydrolyzed/min/mg of protein. This activity was abolished when a conserved lysine in the nucleotide-binding motif was altered. The substrate specificity was low; UTP, CTP, ATP, GTP, dATP, and dGTP served as substrates, UTP having the highest activity of these in vitro. Based on sedimentation equilibrium and size exclusion chromatography, PilT was identified as a approximate to5- to 6-subunit oligomer. Potential implications of the NTPase activity of PilT in pilus retraction are discussed. [References: 44] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Forest KT Univ Wisconsin, Dept Bacteriol 1550 Linden Dr Madison, WI 53706 USA Univ Wisconsin, Dept Bacteriol Madison, WI 53706 USA Univ Wisconsin, Dept Biochem Madison, WI 53706 USA Univ Wisconsin, Biophys Instrumentat Facil Madison, WI 53706 USA <27> UI - 615UU-0040 DD - ISI Document Solution: 615UU AU - Breithaupt DE AU - Bamedi A MA - breithau@uni-hohenheim.de RA - Breithaupt DE TI - Carotenoids and carotenoid esters in potatoes (Solanum tuberosum L.): New insights into an ancient vegetable SO - Journal of Agricultural & Food Chemistry. 50(24):7175-7181, 2002 Nov 20. AS - J. Agric. Food Chem 2002 Nov 20;50(24):7175-7181 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 0021-8561 MH - Potato MH - Solanum tuberosum MH - Carotenoid ester MH - Carotenoid epoxide. MH - Capsicum-annuum l. MH - Pigment MH - Paprika MH - Lutein MH - Phase MH - Serum MH - Flesh MH - Fruit MH - Color MH - Hplc. AB - The carotenoid pattern of four yellow- and four, white-fleshed potato cultivars (Solanum tuberosum. L.), common on the German market, was investigated using HPLC and LC(APCI)=MS for identification and quantification of carotenoids. In each case, the carotenoid pattern was dominated by violaxanthin, antheraxanthin, lutein, and zeaxanthin, which were present in different ratios, whereas neoxanthin, beta-cryptoxanthin, and beta,beta-carotene generally are only minor constituents. In contrast to literature data, antheraxanthiin was found to be the only carotenoid epoxde present in native extracts: The total concentration of the four main carotenoids reached 175 mug/100 g, whereas the sum of carotenoid esters accounted for 41-131 mug/100 g. Therefore, carotenoid esters are regarded as quantitatively. significant compounds in potatoes. For LC(APCI)-MS analyses of carotenoid. esters, a two-stage, cleanup procedure was developed, involving column chromatography on silica gel and enzymatic cleavage of residual triacylglycerides by lipases. This facilitated. the direct identification of several. potato carotenoid esters without previous isolation of the compounds. Although the unequivocal identification of all parent carotenoids was not possible, the cleanup procedure proved to be highly efficient for LC(APCI)-MS analyses of very-low amounts of carotenoid esters. [References: 27] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences Current Contents(R)/Life Sciences CC - Agricultural Chemistry in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Chemistry & Analysis in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Breithaupt DE Univ Hohenheim, Inst Lebensmittelchem Garbenstr 28 D-70593 Stuttgart Germany Univ Hohenheim, Inst Lebensmittelchem D-70593 Stuttgart Germany <28> UI - 617XE-0005 DD - ISI Document Solution: 617XE AU - Massart F AU - Paolini S AU - Piscitelli E AU - Brandi ML AU - Solaini G RA - Massart F TI - Dose-dependent inhibition of mitochondrial ATP synthase by 17 beta-estradiol SO - Gynecological Endocrinology. 16(5):373-377, 2002 Oct. AS - Gynecol. Endocrinol 2002 Oct;16(5):373-377 PU - PARTHENON PUBLISHING GROUP, RICHMOND HOUSE, WHITE CROSS, SOUTH ROAD, LANCASTER LA1 4XQ, ENGLAND. URL: http://www.parthpub.com IS - 0951-3590 MH - Mitochondria MH - Atp synthase MH - Estradiol MH - Apoptosis MH - Non-genomic effect. MH - Cytochrome-c MH - Cell-line MH - Rat-brain MH - Apoptosis MH - Necrosis MH - Bcl-2 MH - Subunit MH - Complex MH - Diethylstilbestrol MH - Purification. AB - Mitochondria produce energy through oxidative phosphorylation. A key enzyme in this pathway is F0F1-ATP synthase, catalyzing ATP production from ADP and inorganic phosphate. Recently a subunit Of F0F1-ATP synthase, oligomycin sensitivity-conferring protein, was identified as a new estradiol-bin ding protein. Estradiol could directly modulate mitochondrial ATP-synthase activity through this subunit. In addition, intracellular ATP levels play a role in apoptotic death, which is an energy-dependent process requiring functioning mitochondria. Here we examined the effect of 17beta-estradiol on F0F1-ATP synthase directly On permeabilized cells) and in intact osteoclastic FLG 29.1 cells, a model of inducible apoptosis. The baseline F0F1-ATP synthase activity of FLG 29.1 cells was 4.485 nmol/min per mg. Estradiol rapidly inhibited F0F1-ATP synthase activity in the physiological range (half-inhibition concentration, IC50, of 30 nmol/l). With 1 nmol/l of estradiol, the inhibition was already significant (8-10% inhibition., p < 0.01) and with 100 nmol/l residual enzyme activity was only 15% (85% inhibition, p < 0.01). In addition, the effect of estradiol appeared to be directed towards F0F1-ATP synthase, since succinate-sustained respiration, uncoupled from the electron transport chain, was unaffected by estradiol. We assayed F0F1-ATP synthase activity in FLG 29.1 cells during inducible apoptosis. No significant difference of ATP synthesis was detected in apoptotic cells versus controls. In conclusion, we showed a new non-genomic effect of estradiol on a key mitochondrial enzyme, which thereby directly modulates cellular energy metabolism. [References: 33] LG - English PT - Article SB - Current Contents(R)/Clinical Medicine CC - Reproductive Medicine in Current Contents(R)/Clinical Medicine. EW - 2002 week 51 IN - Reprint available from: Massart F Scuola Super St Anna Via G Carducci 40 I-56127 Pisa Italy Univ Pisa, Scuola Super Studi & Perfezionamento S Anna Pisa Italy <29> UI - 616ZK-0011 DD - ISI Document Solution: 616ZK AU - White CM RA - White CM TI - HMG CoA reductase inhibitor-induced muscle toxicity: risks, monitoring, and management SO - Hospital Formulary. 37(11):583-588, 2002 Nov. AS - Formulary 2002 Nov;37(11):583-588 PU - ADVANSTAR COMMUNICATIONS, 131 W FIRST ST, DULUTH, MN 55802 USA. URL: http://www.advanstar.com/ IS - 1082-801X MH - Induced rhabdomyolysis MH - Simvastatin treatment MH - Skeletal-muscle MH - Lovastatin MH - Proliferation MH - Pravastatin MH - Ubiquinone MH - Features MH - Exercise. AB - Although the commonly used HMG CoA reductase inhibitors (statins) are well-tolerated and relatively safe, muscle toxicity and rhabdomyolysis can occur with administration and can be severe, accounting for some drug-related deaths. This risk is higher with more bioavailable and lipophilic statins. Concomitant administration of statins with drugs, supplements, or foods that inhibit CYP3A4 or with fibric acid derivates also increases this risk. In addition, advanced age and other clinical factors may predispose a patient to this adverse event. This article summarises what is known about the etiology of statin-associated muscle toxicity, the risks for each statin, and the current recommendations for monitoring and management. [References: 36] LG - English PT - Article SB - Current Contents(R)/Clinical Medicine CC - Pharmacology/Toxicology in Current Contents(R)/Clinical Medicine. EW - 2002 week 51 IN - Reprint available from: White CM Univ Connecticut, Sch Pharm Storrs, CT 06269 USA Univ Connecticut, Sch Pharm Storrs, CT 06269 USA Hartford Hosp, Cardiovasc Pharmacol Serv, Drug Informat Ctr Hartford, CT 06115 USA <30> UI - 616BT-0008 DD - ISI Document Solution: 616BT AU - Berg IA AU - Filatova LV AU - Ivanovsky RN MA - ruslan@protein.bio.msu.su RA - Ivanovsky RN TI - Inhibition of acetate and propionate assimilation by itaconate via propionyl-CoA carboxylase in isocitrate lyase-negative purple bacterium Rhodospirillum rubrum SO - FEMS Microbiology Letters. 216(1):49-54, 2002 Oct 29. AS - FEMS Microbiol. Lett 2002 Oct 29;216(1):49-54 PU - ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS. URL: http://www.elsevier.nl IS - 0378-1097 MH - Citramalate cycle MH - Itaconate MH - Propionyl-coa carboxylase MH - Rhodospirillum rubrum. MH - Microbial metabolism MH - Glyoxylate cycle MH - C2 compounds MH - Pseudomonas-am1 MH - Glycollate MH - Oxidation MH - Operation MH - Ethanol MH - C1. AB - Itaconate is known as a potent inhibitor of isocitrate lyase. Unexpectedly, itaconate was a strong inhibitor of acetate and propionate assimilation in isocitrate lyase-negative purple non-sulfur bacterium Rhodospirillum rubrum. It was shown that in cell extracts of R. rubrum itaconate inhibited propionyl-CoA carboxylase (PCC) activity. The participation of PCC in propionate assimilation in R. rubrum is well-documented, but the inhibition of acetate assimilation suggests that PCC is also involved in acetate metabolism. PCC is one of the enzymes of the citramalate cycle, the anaplerotic pathway proposed for R. rubrum as a substitute for the glyoxylate cycle. These results provide further support for the hypothesis of the occurrence of the citramalate cycle in R. rubrum. PCC from other isocitrate lyase-negative phototrophs; Rhodobacter sphaeroides and Phaeospirillum fulvum, was not inhibited by itaconate. (C) 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. [References: 38] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Microbiology in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Ivanovsky RN Moscow MV Lomonosov State Univ, Dept Microbiol Moscow 119899 Russia Moscow MV Lomonosov State Univ, Dept Microbiol Moscow 119899 Russia <31> UI - 617UA-0005 DD - ISI Document Solution: 617UA AU - Thomson LR AU - Toyoda Y AU - Delori FC AU - Garnett KM AU - Wong ZY AU - Nichols CR AU - Cheng KM AU - Craft NE AU - Dorey CK MA - kdorey@earth.link.net RA - Dorey CK TI - Long term dietary supplementation with zeaxanthin reduces photoreceptor death in light-damaged Japanese quail SO - Experimental Eye Research. 75(5):529-542, 2002 Nov. AS - Exp. Eye Res 2002 Nov;75(5):529-542 PU - ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND. URL: http://www.apnet.com IS - 0014-4835 MH - Zeaxanthin MH - Carotenoid MH - Macular pigment MH - Apoptosis MH - Photoreceptor MH - Light damage MH - Lutein MH - Tocopherol MH - Age-related macular degeneration MH - Age-related maculopathy. MH - Age-related maculopathy MH - Pigment epithelial-cells MH - Outer segment membranes MH - Cone oil droplets MH - Macular degeneration MH - Visual pigments MH - Alpha-tocopherol MH - Apoptotic bodies MH - Oxidative damage MH - Optical-density. AB - The purpose of these studies was to evaluate the effects of light damage on Japanese quail whose retinal carotenoids had been experimentally manipulated through altered diets. The birds were raised 6 months on a commercial turkey diet (T), on a custom carotenoid-deficient diet (C-) containing 90% less carotenoid than the T diet, or on Z+ diet [the C- diet supplemented with natural zeaxanthin (35 mg kg(-1) food)]. Equal numbers of males and females on each diet were exposed to nine intervals (1 hr on, 2 hr off) of 3200 lux cool white light, then placed in the dark for 14 hr before tissue collection. One retina was immediately frozen for HPLC analysis; the other eye was immediately fixed and processed for microscopy. There were no significant differences in the retinal carotenoid concentrations in hatch-mates that were and were not exposed to light. Supplementation resulted in three- to four-fold increases in retinal zeaxanthin and no change in retinal lutein or a-tocopherol, but the C- diet did not reduce the retinal carotenoid concentration in C- birds below that in T birds. The light-exposed retinas had significant numbers of apoptotic photoreceptors and photoreceptor ghosts. The number of ghosts was negatively correlated with the number of dying photoreceptors (P < 0.05), and with retinal concentrations of zeaxanthin, alpha-tocopherol or gamma-tocopherol (P < 0.04, 0.02, 0.04, respectively), but not with lutein. The number of dying photoreceptors was positively correlated with alpha-tocopherol and the sum alpha-tocopherol plus zeaxanthin (P < 0.1; P < 0.04). Photoreceptor death was semi-quantitatively scored, assuming that ghosts were formed by removal of apoptotic photoreceptors with nuclear condensation. Stepwise regression produced a good model (r(2) = 0.67; P < 0.0001) for predicting death scores from retinal concentrations of zeaxanthin (Standard Coefficient = -0.76) and lutein (Standard Coefficients = +0.43). Absence of lutein in gender-specific analyses suggests lutein served as surrogate marker for gender. Combined analysis of the C- and T birds also demonstrated that dying photoreceptors were negatively correlated with retinal zeaxanthin. These data confirm our previous report that retinal carotenoids prevent photoreceptor cell death, and provide the first direct evidence that retinal zeaxanthin protects photoreceptors from light-induced death. (C) 2002 Published by Elsevier Science Ltd. [References: 69] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Medical Research, Organs & Systems in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Dorey CK R&D Consulting 15 Draper Ave Arlington, MA 02474 USA Harvard Univ, Sch Med, Schepens Eye Res Inst Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Ophthalmol Boston, MA 02115 USA Columbia Univ, Sch Med New York, NY 10027 USA Appl Food Biotechnol Inc Ofallon, MO USA Univ British Columbia, Dept Anim Sci Vancouver BC V5Z 1M9 Canada Craft Technol Inc Wilson, NC USA <32> UI - 615ZP-0011 DD - ISI Document Solution: 615ZP AU - Takami S AU - Kawai T AU - Irie M MA - takami@cstf.kyushu-u.ac.jp, tkawai@cstf.kyushu-u.ac.jp, irie@cstf.kyushu-u.ac.jp RA - Irie M TI - Photochromism of dithiazolylethenes having methoxy groups at the reaction centers SO - European Journal of Organic Chemistry. (22):3796-3800, 2002 Nov. AS - Eur. J. Org. Chem 2002 Nov;(22):3796-3800 PU - WILEY-V C H VERLAG GMBH, PO BOX 10 11 61, D-69451 WEINHEIM, GERMANY. URL: http://www.wiley-vch.de IS - 1434-193X MH - Diarylethenes MH - Cyclizations MH - Photochemistry MH - Photochromism. MH - Radiation-induced coloration MH - Dithienylethene derivatives MH - Aryl groups MH - Diarylethenes MH - Cycloreversion MH - Substituents MH - Fulgides MH - Systems. AB - Photochromic dithiazolylethenes [1,2-bis(5-methoxy-2-phenylthiazol-4-yl)perfluorocyclopentene (1a) and (5-methoxy-2phenylthiazol-4-yl) -2-(5-methyl-2-phenylthiazol-4-yl)perfluorocyclopentene (2a)] having methoxy substituents at the reaction centers were synthesized and their photochromic reactivity was compared with 1,2-bis(5-methyl-2-phenylthiazol-4-yl)perfluorocyclopentene (3a), which has methyl substituents at the reaction centers. All dithiazolylethene derivatives underwent reversible photocyclization reactions from the open-ring forms la, 2a, and 3a to the closed-ring forms 1b, 2b, and 3b, respectively. The photocyclization quantum yields of la and 2a were only slightly lower than that of 3a, while the photocycloreversion quantum yields of 1b and 2b dramatically decreased relative to that of 3b by factors of 100 and 10, respectively. Absorption maxima of dithiazolylethene derivatives 1b, 2b, and 3b showed a hypsochromic shift as much as 50-80 nm relative to that of dithienylethene derivatives. This is explained by the difference in the HOMO-LUMO band gap between the two systems. [References: 21] LG - English PT - Article SB - Current Contents(R)/Physical, Chemical & Earth Sciences CC - Organic Chemistry/Polymer Science in Current Contents(R)/Physical, Chemical & Earth Sciences. EW - 2002 week 51 IN - Reprint available from: Irie M Kyushu Univ, Grad Sch Engn, Dept Chem & Biochem, Higashi Ku 6-10-1 hakozaki Fukuoka 8128581 Japan Kyushu Univ, Grad Sch Engn, Dept Chem & Biochem, Higashi Ku Fukuoka 8128581 Japan Japan Sci & Technol Corp, CREST, Higashi Ku Fukuoka 8128581 Japan Fukuoka IST, Fukuoka Ind Sci & Technol Fdn, Higashi Ku Fukuoka 8128581 Japan <33> UI - 614PL-0008 DD - ISI Document Solution: 614PL AU - Hojerslev NK AU - Aarup T MA - nkh@gfy.ku.dk, t.aarup@unesco.org RA - Hojerslev NK TI - Optical measurements on the Louisiana Shelf off the Mississippi River SO - Estuarine Coastal & Shelf Science. 55(4):599-611, 2002 Oct. AS - Estuar. Coast. Shelf Sci 2002 Oct;55(4):599-611 PU - ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND. URL: http://www.apnet.com IS - 0272-7714 MH - Optical measurements MH - Jerlov water types MH - Uv-b irradiance measurements MH - Cdom MH - Mississippi river MH - Louisiana shelf. MH - Remote-sensing reflectance MH - Water MH - Coefficients MH - Radiation MH - Color MH - Model MH - Sea. AB - Optical measurements (UV-B downward irradiance (E-d(310)), photosynthetically available radiation (PAR), light scattering b(655), beam attenuation c(631), ratios of nadir upward radiances (i.e. colour-index), Secchi disc depth and chlorophyll a fluorescence) and CTD measurements were gathered along a cross shelf transect at approximately 92degreesW on the Louisiana Shelf during one cruise in April 1987 and two cruises in February and July 1988. Large cross shelf variability in the optical properties was found over a relatively small spatial scale of about 150 km. In terms of optical water mass classification, Jerlov coastal water type 7 was found near the coast while Jerlov oceanic water type IB was predominant at the shelf edge. The UV-B irradiance measurements showed a negative correlation with salinity which points to the Mississippi and Atchafalaya rivers as a major source of coloured dissolved organic matter (CDOM) in the region. Very clear water was found on the shelf edge in July 1988 and extremely high UV-B irradiance transmission was measured. The 1%-depth for UV-B downward irradiance was 65.2 m, corresponding to a K-d(310)-value of 0.0706 m(-1). This value is approximately 50% lower than the pure water value, K-w(310) of 0.116 m(-1) as given by Smith and Baker (Applied Optics, 20, 177-184) and often used in inverse methods. This result suggests that absorption in the UV-B region by pure water should be re-examined. (C) 2002 Elsevier Science Ltd. All rights reserved. [References: 26] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences CC - Aquatic Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. EW - 2002 week 51 IN - Reprint available from: Hojerslev NK Niels Bohr Inst Anat Phys & Geophys Juliane Maries Vej 30 DK-2100 Copenhagen O Denmark Niels Bohr Inst Anat Phys & Geophys DK-2100 Copenhagen O Denmark <34> UI - 614PL-0009 DD - ISI Document Solution: 614PL AU - Pfannkuche J MA - j.pfannkuche@gmx.de RA - Pfannkuche J TI - Optical properties of Otago shelf waters: South Island New Zealand SO - Estuarine Coastal & Shelf Science. 55(4):613-627, 2002 Oct. AS - Estuar. Coast. Shelf Sci 2002 Oct;55(4):613-627 PU - ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND. URL: http://www.apnet.com IS - 0272-7714 MH - Optical properties MH - Light attenuation MH - Reflectance MH - Scattering MH - Absorption MH - Coastal water MH - Otago MH - New zealand. MH - Yellow substance MH - Underwater light MH - Clarity MH - Attenuation MH - Absorption MH - Coastal MH - Ocean MH - Color MH - Phytoplankton MH - Coefficients. AB - The optical properties and concentrations of optically active water components were measured at 31 stations on the Otago coast. For the broad-band (PAR), diffuse light attenuation decreased 15-fold (K-d=0.76 to 0.05 m(-1)) and reflectance 7-fold (R = 11.95 to 1.45%) from the most turbid harbour water to the clearest oceanic sites 30 km offshore. The K-d values therefore suggested, that Otago shelf waters were appreciably clearer than at first thought. The absorption and scattering coefficients (a and b, respectively) for PAR were calculated using published nomograms. Multiple linear regression showed the dependence of a and b on changes in the concentration of gilvin, g(440), chlorophyll a, [C], and inorganic particles, [I]: a(PAR) = 0.019 + 0.221g(440) + 0.037[C] + 0.018[I] b(PAR) = 0.239[C] + 0.342 [I] Substituting the mean concentrations of gilvin (0.078 m(-1)), chlorophyll a (1.58 mg m(-3)) and inorganic particles (3.23 g m(-3)) into the above equations suggested that gilvin absorbed 11%, phytoplankton 39%, inorganic particles 38% and water itself 12% of PAR and on average. Phytoplankton cells caused 25% and inorganic sediments 75% of the scattering. Spectral irradiance measurements showed, that absorption by gilvin and suspended sediments could dominate absorption in the blue-green waveband for the most turbid harbour waters. Gilvin and phytoplankton levels were lowest in winter and inorganic sediment concentration were generally low offshore (<1 g m(-3)). Thus, oceanic waters were clearer and brighter in winter when compared to spring (July: K-d = 0.05 m(-1); R = 3.1%; November: K-d = 0.11 m(-1); R = 2.1% on average). However, spectral irradiance measurements showed anomalous features in R(lambda) and K-d(lambda) spectra above similar to590 nm which suggested light emission resulting from Raman scattering and chlorophyll fluorescence. (C) 2002 Elsevier Science Ltd. All rights reserved. [References: 40] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences CC - Aquatic Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. EW - 2002 week 51 IN - Reprint available from: Pfannkuche J Ceciliengarten 6 D-12159 Berlin Germany Univ Otago, Dept Marine Sci Dunedin New Zealand <35> UI - BV53C-0008 DD - ISI Document Solution: BV53C AU - Yoshikawa S RA - Yoshikawa S TI - Cytochrome c oxidase [Review] ED - Valentine JS, Gralla EB SO - COPPER-CONTAINING PROTEINS. 60 PG. 341-395. 2002 [Figures]. AS - Adv.Protein Chem 2002;60:341-395 PU - ACADEMIC PRESS INC, 525 B STREET, SUITE 1900, SAN DIEGO, CA 92101-4495 USA. URL: http://www.apnet.com ST - ADVANCES IN PROTEIN CHEMISTRY BI - ACADEMIC PRESS INC, 525 B STREET, SUITE 1900, SAN DIEGO, CA 92101-4495 USA, Hardbound: ISBN 0-12-034260-X, $119.95 IS - 0065-3233 MH - Circular-dichroism spectroscopy MH - Ftir difference spectroscopy MH - Transform infrared-spectroscopy MH - Electron-paramagnetic-resonance MH - Carbon-monoxide binding MH - Heme-copper oxidases MH - Bovine heart MH - Paracoccus-denitrificans MH - Rhodobacter-sphaeroides MH - Proton pump. LG - English PT - Review SB - Current Contents(R)/Life Sciences CC - Current Book Contents in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Yoshikawa S Himeji Inst Technol, Dept Life Sci Kamigohri Akoh Hyogo 6781297 Japan Himeji Inst Technol, Dept Life Sci Kamigohri Akoh Hyogo 6781297 Japan JST, CREST Kamigohri Akoh Hyogo 6781297 Japan <36> UI - 617WP-0008 DD - ISI Document Solution: 617WP AU - Weiss R AU - Fischer J AU - Bulach V AU - Shelnutt JA MA - weiss@chimie.u-strasbg.fr, fischer@chimie.u-strasbg.fr, bulach@chimie.u-strasbg.fr, jasheln@unm.edu RA - Weiss R TI - Molecular structures and mixed spin states of chloroiron(III) complexes of the 2,3-diethyl(detpp), 2,3,7,8-tetraethyl-(cis-tetpp), 2,3,12,13-tetraethyl-(trans-tetpp) and 2,3,7,8,12,13-hexaethyl-(hetpp) 5,10,15,20-tetraphenylporphyrin complexes SO - Comptes Rendus Chimie. 5(5):405-416, 2002 May. AS - C. R. Chim 2002 May;5(5):405-416 PU - EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER, 23 RUE LINOIS, 75724 PARIS CEDEX 15, FRANCE. URL: http://www.elsevier.nl IS - 1631-0748 MH - Iron porphyrins MH - Quantum-mechanically admixed spin states MH - X-ray crystallography MH - Electron paramagnetic resonance MH - Normal coordinate structural decomposition. MH - Ferric cytochrome c' MH - Rhodospirillum-molischianum MH - Photosynthetic bacteria MH - 3-dimensional structure MH - Nonplanar porphyrins MH - Iron(iii) porphyrins MH - Ferricytochrome c' MH - Resolution MH - Peroxidase MH - Conformation. AB - The chloroiron(III) complexes of the partially peripherally crowded 2,3-diethyl-2,3,12,13-tetraethyl-, 2,3,7,8-tetraethyl-, and 2,3,7,8,12,13-hexaethyl-5,10,15,20-tetraphenylporphyrins have been synthesised and their X-ray structures have been determined. The porphyrins present in these molecules are non-planar and assume asymmetric predominately saddle shapes. They are also slightly ruffled and domed according to an analysis of the out-of-plane distortions performed by using normal-coordinate structural decomposition (NSD). The saddle deformations, dominant in these chloroiron(III) complexes, are larger than those observed in all the cytochromes c', whose structures were analysed by this method. Despite the large saddle-shaped distortions of the porphyrins present in these species, the quantum mechanical S = 3/2 spin admixtures into the S = 5/2 high-spin state (QMS state) observed are small. The EPR spectra of these C-beta-ethyl-substituted tetraphenylporphyrin complexes indicate S = 3/2 admixtures of 0% in Fe(detpp)Cl (1), 0.75% in Fe(trans-tetpp)Cl (2), 1.20% in Fe(cis-tetpp)Cl (3) and 2.75% in Fe(hetpp)Cl (4). The large saddle distortions of the porphyrins present in these compounds and the small S = 5/2,3/2 spin admixtures found indicate that the saddle distortions alone are probably not sufficient to cause the QMS states observed in several ferricytochromes c' isolated from photosynthetic bacteria and in plant peroxidases. [References: 34] LG - English PT - Article SB - Current Contents(R)/Physical, Chemical & Earth Sciences CC - Chemistry in Current Contents(R)/Physical, Chemical & Earth Sciences. EW - 2002 week 51 IN - Reprint available from: Weiss R Univ Strasbourg 1, ISIS, Lab Chim Supramol, UMR 7006 CNRS 4 Rue Blaise Pascal F-67070 Strasbourg France Univ Strasbourg 1, ISIS, Lab Chim Supramol, UMR 7006 CNRS F-67070 Strasbourg France Univ Strasbourg 1, Inst Le Bel, Lab Chim Organomet & Catalyse, UMR 7513 F-67070 Strasbourg France Univ Strasbourg 1, Inst Le Bel, Lab Chim Coordinat Organ, UMR 7513 F-67070 Strasbourg France Sandia Natl Labs, Biomol Mat & Interfaces Dept Albuquerque, NM 87185 USA <37> UI - 616QV-0053 DD - ISI Document Solution: 616QV AU - Cuezva JM AU - Krajewska M AU - de Heredia ML AU - Krajewski S AU - Santamaria G AU - Kim H AU - Zapata JM AU - Marusawa H AU - Chamorro M AU - Reed JC MA - jmcuezva@cbm.uam.es RA - Cuezva JM TI - The bioenergetic signature of cancer: A marker of tumor progression SO - Cancer Research. 62(22):6674-6681, 2002 Nov 15. AS - Cancer Res 2002 Nov 15;62(22):6674-6681 PU - AMER ASSOC CANCER RESEARCH, PO BOX 11806, BIRMINGHAM, AL 35202 USA. URL: http://www.aacr.org IS - 0008-5472 MH - Beta-f1-atpase messenger-rna MH - Hypoxia-inducible factor-1-alpha MH - Oxidative-phosphorylation MH - Mitochondrial biogenesis MH - Atp synthase MH - Translational efficiency MH - 3'-untranslated region MH - Coactivator pgc-1 MH - Gene-expression MH - Factor 1-alpha. AB - Mitochondrial H+-ATP synthase is required for cellular energy provision and for efficient execution of apoptosis. Almost one century ago, Otto Warburg proposed the hypothesis that mitochondrial function might be impaired in cancer cells. However, his hypothesis was never demonstrated in human carcinomas. In this study, we have analyzed the expression of the beta-catalytic subunit of the H+-ATP synthase (beta-F1-ATPase) of mitochondria in carcinomas of the human liver, kidney, and colon. We show that carcinogenesis in the liver involves a depletion of the cellular mitochondrial content, as revealed by reduced content of mitochondrial markers, whereas in kidney and colon carcinomas, it involves a selective repression of the expression of the beta-F1-ATPase concurrent with an increase in the expression of the glycolytic glyceraidehyde-3-phosphate dehydrogenase. Both mechanisms limit mitochondrial cellular activity in cancer, strongly supporting Warburg's hypothesis, and suggest a mechanism for the resistance and compromised apoptotic potential of tumor cells. Furthermore, we show that the metabolic state of the cell, as defined by a bioenergetic mitochondrial index relative to the cellular glycolytic potential, provides a signature of carcinogenesis of prognostic value in assessing the progression of colorectal carcinomas. [References: 40] LG - English PT - Article SB - Current Contents(R)/Clinical Medicine Current Contents(R)/Life Sciences CC - Oncology in Current Contents(R)/Clinical Medicine. Oncogenesis & Cancer Research in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Cuezva JM Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa, CSIC, Dept Mol Biol E-28049 Madrid Spain Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa, CSIC, Dept Mol Biol E-28049 Madrid Spain Yonsei Univ, Coll Med, Dept Pathol Seoul South Korea Burnham Inst La Jolla, CA 92037 USA <38> UI - 615FQ-0005 DD - ISI Document Solution: 615FQ AU - Li HP AU - Gong GC AU - Hsiung TM MA - tmhsiung@mail.ntou.edu.tw RA - Hsiung TM TI - Phytoplankton pigment analysis by HPLC and its application in algal community investigations SO - Botanical Bulletin of Academia Sinica. 43(4):283-290, 2002 Oct. AS - Bot. Bul. Acad. Sin 2002 Oct;43(4):283-290 PU - ACAD SINICA INST BOTANY, NANKANG, TAIPEI 11529, TAIWAN. URL: http://www.botany.sinica.edu.tw/ IS - 0006-8063 MH - Algal community MH - Hplc MH - Marker pigments MH - Phytoplankton. MH - East-china-sea MH - Divinyl chlorophyll-a MH - Seasonal-variation MH - North-atlantic MH - Ocean MH - Equations MH - Carbon. AB - A high performance liquid chromatography (HPLC) system for pigment analysis of marine phytoplankton was established. The characteristic quantification limits of the major photosynthetic chlorophylls a and b were 0.29 and 0.27 ng, respectively. The reliability of this method was verified by resolving the marker pigments in culture extracts from diatoms, blue-green algae and green algae. Fucoxanthin, zeaxanthin and chlorophyll b were selected for calculating the chlorophyll a/marker pigment ratios for the three types of algae, which were 1.39, 0.51 and 1.01, respectively. The composition of the phytoplankton community in summer samples, collected from the continental shelf of the East China Sea, was estimated by simple regression of these ratios. When results of composition abundance of diatoms and blue-green algae obtained by this method were compared with those obtained by the microscopic technique, the relative percentage difference was less than 6% for diatoms. On the other hand, a lower abundance of blue-green algae was estimated by the HPLC method. [References: 32] LG - English PT - Article SB - Current Contents(R)/Agriculture, Biology & Environmental Sciences CC - Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences. EW - 2002 week 51 IN - Reprint available from: Hsiung TM Natl Taiwan Ocean Univ, Inst Biosci & Biotechnol Chilung 202 Taiwan Natl Taiwan Ocean Univ, Inst Biosci & Biotechnol Chilung 202 Taiwan Natl Taiwan Ocean Univ, Dept Oceanog Chilung 202 Taiwan <39> UI - 617RU-0003 DD - ISI Document Solution: 617RU AU - Braun V AU - Patzer SI AU - Hantke K MA - volkmar.braun@mikrobio.uni-tuebingen.de RA - Braun V TI - Ton-dependent colicins and microcins: modular design and evolution SO - Biochimie. 84(5-6):365-380, 2002 May-Jun. AS - Biochimie 2002 May-Jun;84(5-6):365-380 PU - EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER, 23 RUE LINOIS, 75724 PARIS CEDEX 15, FRANCE. URL: http://www.elsevier.nl IS - 0300-9084 MH - Colicins b, d, g, h, i, js, m, v, 5, 10 MH - Pesticin MH - Microcins e492, 24, j25, h47, m. MH - Escherichia-coli MH - Immunity protein MH - Outer-membrane MH - Crystal-structure MH - Inner membrane MH - Export system MH - Salmonella-typhimurium MH - Functional-properties MH - Nucleotide-sequence MH - Genetic-analysis. AB - Ton-dependent colicins and microcins are actively taken up into sensitive cells at the expense of energy which is provided by the proton motive force of the cytoplasmic membrane. The Ton system consisting of the proteins TonB, ExbB and ExbD is required for colicin and microcin import. Colicins as well as the outer membrane transport proteins contain proximal to the N-terminus a short sequence, called TonB box, which interacts with TonB and in which point mutants impair uptake. No TonB box is found in microcins. Colicins are composed of functional modules which during evolution have been interchanged resulting in new colicins. The modules define sites of interaction with the outer membrane transport genes, TonB, the immunity proteins, and the activity regions. Six TonB-dependent microcins with different primary structures are processed and exported by highly homologous proteins. Three of these microcins are modified in an unknown way and they have in common specificity for catecholate siderophore receptors. (C) 2002 Societe francaise de biochimie et biologic moleculaire / Editions scientifiques et medicales Elsevier SAS. All rights reserved. [References: 78] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Braun V Univ Tubingen Morgenstelle 28 D-72076 Tubingen Germany Univ Tubingen D-72076 Tubingen Germany <40> UI - 617RU-0022 DD - ISI Document Solution: 617RU AU - Hechard Y AU - Sahl HG MA - yann.hechard@univ-poitiers.fr RA - Hechard Y TI - Mode of action of modified and unmodified bacteriocins from Gram-positive bacteria SO - Biochimie. 84(5-6):545-557, 2002 May-Jun. AS - Biochimie 2002 May-Jun;84(5-6):545-557 PU - EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER, 23 RUE LINOIS, 75724 PARIS CEDEX 15, FRANCE. URL: http://www.elsevier.nl IS - 0300-9084 MH - Bacteriocin MH - Lantibiotic MH - Antibacterial MH - Pore. MH - Lactic-acid bacteria MH - Peptide antibiotic nisin MH - Sodium dodecyl-sulfate MH - Enterococcus-faecium t136 MH - Precursor lipid ii MH - Listeria-monocytogenes MH - Pediocin pa-1 MH - Pore-formation MH - Pediococcus-acidilactici MH - Phospholipid-vesicles. AB - The antibiotic activity of bacteriocins from Gram-positive bacteria, whether they are modified (class I bacteriocins, lantibiotics) or unmodified (class II), is based on interaction with the bacterial membrane. However, recent work has demonstrated that for many bacteriocins, generalised membrane disruption models as elaborated for amphiphilic peptides (e.g. tyriodal pore or carpet model) cannot adequately describe the bactericidal action. Rather, specific targets seem to be involved in pore formation and other activities. For the nisin and epidermin family of lantibiotics, the membrane-bound cell wall precursor lipid II has recently been identified as target. The duramycin family of lantibiotics binds specifically to phosphoethanolamine which results in inhibition of phospholipase A2 and various other cellular functions. Most of the class II bacteriocins dissipate the proton motive force (PMF) of the target cell, via pore formation. The subclass IIa bacteriocin activity likely depends on a mannose permease of the phosphotransferase system (PTS) as specific target. The subclass IIb bacteriocins (two-component) also induce dissipation of the PMF by forming cation- or anion-specific pores; specific targets have not yet been identified. Finally, the subclass IIc comprises miscellaneous peptides with various modes of action such as membrane permeabilisation, specific inhibition of septum formation and pheromone activity. (C) 2002 Societe francaise de biochimie et biologie moleculaire / Editions scientifiques et medicales Elsevier SAS. All rights reserved. [References: 87] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Hechard Y Univ Poitiers, Lab Fundamental & Appl Microbiol 40 Ave Recteur Pineau F-86022 Poitiers France Univ Poitiers, Lab Fundamental & Appl Microbiol F-86022 Poitiers France Univ Bonn, Inst Med Microbiol & Immunol D-53127 Bonn Germany <41> UI - 616CH-0010 DD - ISI Document Solution: 616CH AU - Harrison M AU - Singh SM MA - ssingh@uwo.ca RA - Singh SM TI - Genetics and differential expression of NADH : ubiquinone oxidoreductase B8 subunit in brains of genetic strains of mice differing in voluntary alcohol consumption SO - Biochimica et Biophysica Acta - Gene Structure & Expression. 1579(2-3):164-172, 2002 Dec 12. AS - Biochim. Biophys. Acta-Gene Struct. Expression 2002 Dec 12;1579(2-3):164-172 PU - ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS. URL: http://www.elsevier.nl IS - 0167-4781 MH - Genetics MH - Nadh : ubiquinone oxidoreductase MH - Alcohol. MH - Polymerase chain-reaction MH - Central-nervous-system MH - Messenger-rna MH - Chronic ethanol MH - Rat-brain MH - Proteins MH - Nuclear MH - Heart MH - Metabolism MH - Stress. AB - Inbred strains of mice remain a valuable resource for genetic dissection of complex traits including responses to drugs and chemicals, particularly alcohol. As a novel source of candidate genes for further analysis, we have used mRNA differential displays to identify genes with differential expression in the brains of ethanol-preferring (C57BL/6J) vs. ethanol-avoiding (A/J, BALB/c, and DBA/2J) strains, with and without ethanol i.p. treatments (4 g/kg). We report on one such gene, NADH:ubiquinone oxidoreductase B8 subunit, that has a higher expression in the C57BL/6J. Further, its expression also increases following ethanol treatment as compared to the three alcohol-avoiding strains. This regulatory feature follows three single nucleotide polymorphisms (SNPs) in the promoter region across the four strains studied. The four strains represent only two haplotypes, one C57BL/6J-specific and the other found in the three alcohol-avoiding strains. Interestingly, one of the observed SNPs (-687 A/G) is located in the putative TFIID binding site with potential to regulate the expression of this gene and contribute to genotype-specific alcohol responses and effects involving reactive oxygen species (ROS). (C) 2002 Elsevier Science B.V. All rights reserved. [References: 29] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Molecular Biology & Genetics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Singh SM Univ Western Ontario, Dept Biol, Mol Genet Unit 307 Western Sci Ctr London ON N6A 5B7 Canada Univ Western Ontario, Dept Biol, Mol Genet Unit London ON N6A 5B7 Canada <42> UI - 615FY-0042 DD - ISI Document Solution: 615FY AU - Hasegawa K AU - Kimura Y AU - Ono TA MA - kojihase@postman.riken.go.jp, takaaki@postman.riken.go.jp RA - Hasegawa K TI - Chloride cofactor in the photosynthetic oxygen-evolving complex studied by Fourier transform infrared spectroscopy SO - Biochemistry. 41(46):13839-13850, 2002 Nov 19. AS - Biochemistry 2002 Nov 19;41(46):13839-13850 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 0006-2960 MH - Electron-paramagnetic-res MH - Water-oxidizing complexes MH - Photosystem-ii membranes MH - S-state dependence MH - Difference spectroscopy MH - Mn-cluster MH - Thylakoid membranes MH - Plastoquinone q(a) MH - Structural-changes MH - Ftir difference. AB - Fourier transform infrared (FTIR) spectroscopy, using midfrequency S-2/S-1 FTIR difference spectra, has been applied to studies of chloride cofactor in the photosynthetic oxygen-evolving complex (OEC) to determine the effects of Cl- depletion and monovalent anion substitution. Cl- depletion resulted in the disappearance of a large part of the amide I and II vibrational modes, and induced characteristic modification in the features of the stretching modes of the carboxylate ligands of the Mn cluster. The normal spectral features were largely restored by replenishment of Cl- except for some changes in amide bands. The overall features of Br--, I--, or NO3--substituted spectra were similar to those of the Cl-reconstituted spectrum, consistent with their ability to support oxygen evolution. In contrast, the spectrum was significantly altered by the replacement of Cl- with F- or CH3COO-, which resulted in marked suppression and distortion of both the carboxylate and amide bands. The activity of oxygen evolution restored by NO3- was as high as that. by Cl- when measured under limited light conditions, indicating that the NO3--substituted OEC is fully active in oxygen evolution, although with a slow turnover rate. The double-difference spectrum between the (NO3-)-N-14-substituted and (NO3-)-N-15-substituted S-2/S-1 difference spectrum showed isotopic bands for asymmetric NO stretching mode in the region of 1400-1300 cm(-1) due to NO3- bound to the Cl- site. This demonstrated structural coupling between the Cl- site and the Mn cluster. A proposed model for the isotopic bands suggested that Cl- as well as NO3- is not directly associated with the Mn cluster and exists in a more symmetric configuration and weaker binding state in the S-2 state than in the S-1 state. These results also suggest that Cl- is required for changes in the structure of the specific carboxylate ligand of the Mn cluster as well as the peptide backbone of protein matrixes upon the transition from S-1 to S-2. [References: 78] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Hasegawa K RIKEN, Photodynam Res Ctr, Inst Phys & Chem Res, Lab Photo Biol 1 519-1399 Aoba Sendai Miyagi 9800845 Japan RIKEN, Photodynam Res Ctr, Inst Phys & Chem Res, Lab Photo Biol 1 Sendai Miyagi 9800845 Japan <43> UI - 617RT-0019 DD - ISI Document Solution: 617RT AU - Yakovlev AG AU - Shkuropatov AY AU - Shuvalov VA MA - shuvalov@issp.serpukhov.su RA - Shuvalov VA TI - Nuclear wave packet motion between P* and P+BA- potential surfaces with a subsequent electron transfer to H-A in bacterial reaction Centers at 90 K. Electron transfer pathway SO - Biochemistry. 41(47):14019-14027, 2002 Nov 26. AS - Biochemistry 2002 Nov 26;41(47):14019-14027 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 0006-2960 MH - Photosynthetic reaction centers MH - Bacteriochlorophyll anion band MH - Resonance raman-spectroscopy MH - Rhodobacter-sphaeroides r-26 MH - Viridis reaction centers MH - Rhodopseudomonas-viridis MH - Accessory bacteriochlorophyll MH - Femtosecond spectroscopy MH - Charge separation MH - Wavepacket motion. AB - In Rhodobacter sphaeroides R-26 reaction centers (RCs) the nuclear wave packet induced by 25 fs excitation at 90 K moves on the primary electron donor P* potential energy hypersurface with initial frequency at similar to130 cm(-1) (monitored by stimulated emission measurement). At the long-wavelength side of P* stimulated emission at 935 nm the wave packet is transferred to the surface with P+BA- character at 120, 380, 1.2 fs, etc. delays (monitored by measurement of the primary electron acceptor B-A(-) band at 1020 nm). However, only beginning from 380 fs delay and later the relative stabilization of the state P+BA- is observed. This is accompanied by the electron transfer to bacteriopheophytin H-A (monitored by H-A band measurement at 760 nm). The most active mode of 32 cm(-1) in the electron transfer and its overtones up to the seventh were found in the Fourier transform spectrum of the oscillatory part of the kinetics of the P* stimulated emission and of the P+BA- and P+HA- formation. This mode and its overtones are apparently populated via the 130 cm(-1) vibrational mode. The deuteration of the sample shifts the fundamental frequency (32 cm(-1)) and all overtones by the same factor of similar to1.3. This mode and its overtones are suppressed by a factor of similar to4.7 in the dry film of RCs. The results obtained indicate that the 32 cm(-1) mode might be related to a rotation of hydrogen-containing groups (possibly the water molecule) participating in the modulation of the primary electron transfer from P* to B-A(-) in at least 35% of RCs. The Brookhaven Protein Data Bank (1PRC) displays the water molecule located at the position HOH302 between His M200 (axial ligand for P-B) and the oxygen of ring V of B-A which might be a part (similar to35%) of the molecular pathway for electron transfer from P* to B-A. [References: 44] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Shuvalov VA Moscow MV Lomonosov State Univ, Dept Photobiophys, Belozersky Inst Chem & Phys Biol Moscow 119992 Russia Moscow MV Lomonosov State Univ, Dept Photobiophys, Belozersky Inst Chem & Phys Biol Moscow 119992 Russia Russian Acad Sci, Inst Basic Biol Problems Pushchino 142290 Moscow Region Russia <44> UI - 617RT-0020 DD - ISI Document Solution: 617RT AU - Nagashima KVP AU - Matsuura K AU - Shimada K AU - Vermeglio A MA - nagashima-kenji@c.metro-u.ac.jp RA - Nagashima KVP TI - High-potential iron-sulfur protein (HiPIP) is the major electron donor to the reaction center complex in photosynthetically growing cells of the purple bacterium Rubrivivax gelatinosus SO - Biochemistry. 41(47):14028-14032, 2002 Nov 26. AS - Biochemistry 2002 Nov 26;41(47):14028-14032 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 0006-2960 MH - Bound cytochrome subunit MH - Rhodopseudomonas-viridis MH - Rhodoferax fermentans MH - Participation MH - C(8). AB - A gene encoding the high-potential iron-sulfur protein (HiPIP) was cloned from the purple photosynthetic bacterium Rubrivivax gelatinosus. An insertional disruption of this gene by a kanamycin resistance cartridge resulted in a significant decrease in the growth rate under photosynthetic growth conditions. Flash-induced kinetic measurements showed that the rate of reduction of the photooxidized reaction center is greatly diminished in the mutant depleted in the HiPIP. On the other hand, mutants depleted in the low- and high-potential cytochromes c(8), the two other soluble electron carriers, which have been shown to donate an electron to the reaction center in Rvi. gelatinosus, showed growth rates similar to those of the wild type under both photosynthetic and respiratory growth conditions. It was concluded that HiPIP is the major physiological electron donor to the reaction center in Rvi. gelatinosus cells grown under photosynthetic conditions. [References: 17] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Nagashima KVP Tokyo Metropolitan Univ, Dept Biol Minamiohsawa 1-1 Hachioji Tokyo 1920397 Japan Tokyo Metropolitan Univ, Dept Biol Hachioji Tokyo 1920397 Japan Univ Mediterranee, DEVM Lab Bioenerget Cellulaire, UMR 163, CNRS,CEA Cadarache F-13108 St Paul Les Durance France <45> UI - 617RT-0023 DD - ISI Document Solution: 617RT AU - Zu YB AU - Fee JA AU - Hirst J MA - jh@mrc-dunn.cam.ac.uk RA - Hirst J TI - Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of Thermus thermophilus: Characterization of the sulfhydryl state by protein-film voltammetry SO - Biochemistry. 41(47):14054-14065, 2002 Nov 26. AS - Biochemistry 2002 Nov 26;41(47):14054-14065 PU - AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA. URL: http://pubs.acs.org IS - 0006-2960 MH - Iron-sulfur protein MH - Site cysteine residues MH - Lumen-side domain MH - Bc(1) complex MH - Ubihydroquinone oxidation MH - Cytochrome-bc(1) complex MH - Rhodobacter-sphaeroides MH - Phthalate dioxygenase MH - Thioredoxin reductase MH - Mutational analysis. AB - A disulfide bond, adjacent to the [2Fe-2S] cluster, is conserved in all high-potential Rieske proteins from the respiratory and photosynthetic cytochrome bc(1) and b(6)f complexes but is absent from the low-potential, bacterial dioxygenase Rieske proteins. The role of the disulfide is unclear, since cysteine mutants have resulted in only apoprotein. The high stability of the soluble Thermus thermophilus Rieske protein permits chemical reduction of the disulfide bond and characterization of the sulfhydryl (dithiol) form by protein-film voltammetry. The effect of disulfide reduction on the cluster potential is small (DeltaE(0)' less than or equal to -0.04 V) and attributed to relaxation of the disulfide tether between the protein loops ligating the cluster, including possible mechanical strain release and hydrogen-bonding modification. Above pH 6 an additional decrease in potential of the sulfhydryl form is assigned to the nearby negatively charged thiolates (DeltaE(0)' -0.16 to -0.12 V); the histidine-ligand nitrogen pKs are correspondingly increased. Entropies of reduction for the native and dithiolate forms are equal (-48 +/- 5 J K-1 mol(-1), pH 7-8); thus changes in reduction potential are enthalpic in origin. Following sulfhydryl alkylation the cluster redox properties mirror those of the native protein (DeltaE(0)' similar to -0.1 V) over all pHs. While a sustained electrode potential of -0.85 V fails to reduce the disulfide, the free sulfhydryls recombine upon an oxidative excursion, at low pH, to restore the native redox properties. This unique behavior is attributed to preorganization of the two thiolate groups upon uptake of one or more protons by the sulfhydryl pair. [References: 65] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Hirst J MRC, Dunn Human Nutr Unit, Wellcome Trust MRC Bldg,Hills Rd Cambridge England MRC, Dunn Human Nutr Unit, Wellcome Trust Cambridge England Univ Calif San Diego, Div Biol La Jolla, CA 92093 USA The Scripps Res Inst, Dept Mol Biol La Jolla, CA 92037 USA <46> UI - 617RK-0012 DD - ISI Document Solution: 617RK AU - Gavin P AU - Devenish RJ AU - Prescott M MA - Mark.Prescott@med.monash.edu.au RA - Prescott M TI - An approach for reducing unwanted oligomerisation of DsRed fusion proteins SO - Biochemical & Biophysical Research Communications. 298(5):707-713, 2002 Nov 15. AS - Biochem. Biophys. Res. Commun 2002 Nov 15;298(5):707-713 PU - ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA. URL: http://www.apnet.com IS - 0006-291X MH - Fluorescent protein MH - Dsred MH - Yeast MH - Atp synthase MH - Oligomerisation. MH - Green fluorescent protein MH - Atp synthase MH - Saccharomyces-cerevisiae MH - Yeast MH - Mitochondria MH - Expression MH - F1-atpase MH - Subunits MH - Complex MH - Oscp. AB - Oligomerisation of the red fluorescent protein, DsRed, can interfere with the localisation and function of proteins to which it is fused. We demonstrate an approach that may help to reduce significantly the impact of oligomerisation on the biology of the protein fusion partner. Growth of yeast (Saccharomyces cerevisiae) cells expressing ATP synthase containing subunit gamma-DsRed fusion was compromised relative to control cells. Furthermore, ATP synthase was found to exist as oligomeric structures when isolated under conditions where monomers would normally be present. The compromised growth phenotype was partially reversed and the oligomerisation of the ATP synthase reduced when a non-fluorescent variant of DsRed not fused to another protein was targeted to the mitochondrion in addition to the gamma-DsRed fusion protein. This strategy may also be applicable to the reduction of unwanted interactions between fusion proteins that contain the normally dimeric fluorescent proteins HcRed or Renilla GFP. (C) 2002 Elsevier Science (USA). All rights reserved. [References: 21] LG - English PT - Article SB - Current Contents(R)/Life Sciences CC - Biochemistry & Biophysics in Current Contents(R)/Life Sciences. EW - 2002 week 51 IN - Reprint available from: Prescott M Monash Univ, Dept Biochem & Mol Biol POB 13D,Calyton Campus Clayton Vic 3800 Australia Monash Univ, Dept Biochem & Mol Biol Clayton Vic 3800 Australia