Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870886 | FEBS Letters | 2013 | 6 Pages |
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.
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Agricultural and Biological Sciences
Plant Science
Authors
Peng Hu, Jing Lv, Pengcheng Fu, Mi Hualing,