Article

Title:Reduction of photosystem I reaction center by recombinant DrgA protein in isolated thylakoid membranes of the cyanobacterium Synechocystis sp. PCC 6803.
Authors:Elanskaya IV; Toporova VA; Grivennikova VG; Muronets EM; Lukashev EP; Timofeev KN
Publication:Biochemistry (Mosc). 2009 Oct;74(10):1080-7.
PubmedID19916920
Abstract
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.