Reduction of Photosystem I Reaction Center by Recombinant DrgA Protein in Isolated Thylakoid Membranes of the Cyanobacterium Synechocystis sp. PCC 6803статья
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Дата последнего поиска статьи во внешних источниках: 20 сентября 2013 г.
Аннотация:To study the function of soluble NAD(P)H:quinone-oxidoreductase of the cyanobacterium Synechocystis sp. PCC 6803 encoded by drgA gene, recombinant DrgA protein carrying 12 histidine residues on the C-terminal end was expressed in Escherichia coli and purified. Recombinant DrgA is a flavoprotein that exhibits quinone reductase and nitroreductase
activities with NAD(P)H as the electron donor. Using EPR spectroscopy, it was demonstrated that addition of recombinant DrgA protein and NADPH to DCMU-treated isolated thylakoid membranes of the cyanobacterium increased the dark re-reduction rate of the photosystem I reaction center (P700+). Thus, DrgA can participate in electron transfer from NADPH
to the electron transport chain of the Synechocystis sp. PCC 6803 thylakoid membrane.