Properties of the Respiratory NAD(P)H Dehydrogenase Isolated from the Cyanobacterium Synechocystis PCC6803
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概要
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Activity staining with NADPH-nitroblue tetrazolium after native-PAGE of membrane proteins of Synechocystis PCC6803, solubilized with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), revealed four NAD(P)H dehydrogenase (NDH) activities; an NDH complex of the respiratory chain, a ferredoxin NADP^+ reductase (FNR), a drgA product which oxidized both NADH and NADPH, and an uncharacterized NADH-specific enzyme. The NDH complex was purified with anion exchange and gel filtration chromatographies. The purified complex had a molecular mass of 376 kDa and was composed of 9 subunits. Western analysis showed that the complex contained the NDH-H subunit, but not NDH-A or B. The enzyme reduced ferricyanide much faster than plastoquinone and used NADPH as its prefered electron donor rather than NADH. The enzymatic activity was inhibited by diphenyleneiodonium chloride and salicylhydroxamic acid, but not by rotenone, p-chloromercuribenzoate, N-ethylmaleimide, flavon, dicumarol, or antimycin A. These results suggest that the purified complex is a hydrophilic subcomplex which contains an NADPH binding site and flavin, and is dissociated from a hydrophobic subcomplex, which contains quinone binding site.
著者
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Matsuo Michinori
Research Institute for Food Science, Kyoto University
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Endo Tsuyoshi
Research Institute for Food Science, Kyoto University
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Asada Kozi
Research Institute for Food Science, Kyoto University
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Matsuo Michinori
Research Institute For Food Science Kyoto University:(present Address)division Of Applied Life Scien
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Asada K
Fukuyama Univ. Hiroshima Jpn
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Asada Kozi
Dept. Biotech Fac. Engin. Fukuyama Univ.
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Asada Kozi
Faculty Of Bioscience And Biotechnology Fukuyama University
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Asada K
The Research Institute For Food Science Kyoto University
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ENDO Tsuyoshi
Kyoto Univ.Food Sci.
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Asada Kozi
The Research Institute For Food Science Kyoto University:(present)department Of Biotechnology Facult
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Endo Tsuyoshi
Department Of Bioresource Science Obihiro University Of Agriculture And Veterinary Medicine
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Endo Tsuyoshi
Department Of Plant Genes And Totipotency Graduate School Of Biostudies Kyoto University
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Asada K
Dept. Biotech Fac. Engin. Fukuyama Univ.
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Asada Kozi
Research Institute For Food Science Kyoto University
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Matsuo Masahiko
Research Institute For Food Science Kyoto University:(present Address)division Of Applied Life Scien
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Endo T
Graduate School Of Biostudies Kyoto University
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Asada Kozu
The Research Institute For Food Science Kyoto University
関連論文
- Properties of the Respiratory NAD(P)H Dehydrogenase Isolated from the Cyanobacterium Synechocystis PCC6803
- MOLECULAR SPECIES OF NADPH-SPECIFIC NDH IN STROMA OF HIGHER PLANTS
- NAD(P)H Dehydrogenase-Dependent, Antimycin A-Sensitive Electron Donation to Plastoquinone in Tobacco Chloroplasts
- Isolation of a Novel NAD(P)H-Quinone Oxidoreductase from the Cyanobacterium Synechocystis PCC6803
- Donation of Electrons to Plastoquinone by NAD(P)H Dehydrogenase and by Ferredoxin-Quinone Reductase in Spinach Chloroplasts
- INHIBITION OF NAD(P)H DEGYDROGENASE (NDH) BY HQNO IN THE CYANOBACTERIUM Synechocystis PCC 6803
- PURIFICATION OF NAD(P)H DEHYDROGENASE COMPLEX (NDH) IN Synechocystis PCC 6803
- CYCLIC ELECTRON TRANSPORT MEDIATED BY NAD(P)H DEHYDROGENASE IN TOBACCO CHLOROPLASTS
- NAD(P)H DEHYDROGENASE-DEPENDENT CYCLIC ELECTRON FLOW AROUND PHOTOSYSTEM I IN CYANOBACTERIA
- INDUCTION AND PURIFICATION OF NAD(P)H DEHYDROGENASE COMPLEX(NDH)IN Synechocystis PCC 6803