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FEBS Lett. 2013 Aug 2;587(15):2340-5. doi: 10.1016/j.febslet.2013.05.040. Epub 2013 May 27.

Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus.

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  • 1National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, CAS, 300 Fenglin Road, Shanghai 200032, China.

Abstract

Although type-1 NAD(P)H dehydrogenase (NDH) complex subunit constituents and physiological functions have been reported in plants and cyanobacteria, the biochemical properties of this enzyme are not clear. We used chromatographic isolation to purify and characterize a NADPH-active NDH from the cyanobacterium Thermosynechococcus elongatus. Ferredoxin (Fd) and ferredoxin-NADP(+) oxidoreductase (FNR) were co-eluted with NDH, implying the electron donation from NADPH to NDH via the interaction with FNR. We investigated the enzymatic properties of the complex. Furthermore, the activity is competitively inhibited by rotenone, suggesting that it possesses a quinone binding site, similar to mitochondria complex I.

Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

KEYWORDS:

2,6-dichloroindophenol sodium salt dydrate; Cyanobacteria; DCPIP; DM; FNR; Fd; Ferredoxin; Ferredoxin NADP(+) oxidoreductase; HEPES; N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid; NADPH oxidation; NDH; NDH complex; PBS; PS I; Q(0); Q(10); Rotenone; ferredoxin; ferredoxin-NADP(+) oxidoreductase; n-dodecyl-β-d-maltoside; photosystem I; phycobilisome protein; type-1 NAD(P)H dehydrogenase; ubiquinone-0; ubiquinone-10

PMID:
23722112
[PubMed - indexed for MEDLINE]
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