Journal Article

Properties of the Respiratory NAD(P)H Dehydrogenase Isolated from the Cyanobacterium <i>Synechocystis</i> PCC6803

Michinori Matsuo, Tsuyoshi Endo and Kozi Asada

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 39, issue 3, pages 263-267
Published in print March 1998 | ISSN: 0032-0781
Published online March 1998 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029366
Properties of the Respiratory NAD(P)H Dehydrogenase Isolated from the Cyanobacterium Synechocystis PCC6803

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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.

Keywords: Complex I; Cyclic electron transport; NAD(P)H dehydrogenase (NDH, EC 1.6.99.3); Photosynthesis; Respiration; SynechocystisPCC6803

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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