Reduction of photosystem I reaction center by recombinant DrgA protein in isolated thylakoid membranes of the cyanobacterium Synechocystis sp. PCC 6803.
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.
Elanskaya
I V
IV
Faculty of Biology, Lomonosov Moscow State University, Moscow, 119992, Russia. ivelanskaya@mail.ru
Toporova
V A
VA
Grivennikova
V G
VG
Muronets
E M
EM
Lukashev
E P
EP
Timofeev
K N
KN
D000595:Amino Acid Sequence; D000458:Cyanobacteria / Q000145:classification; D004579:Electron Transport; D042967:Electron Transport Complex I / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000235:genetics; D009601:Nitroreductases / Q000378:metabolism; D010084:Oxidation-Reduction; D010788:Photosynthesis; D045331:Photosystem I Protein Complex / Q000378:metabolism*; D011808:Quinone Reductases / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D046939:Synechocystis / Q000737:chemistry* / Q000378:metabolism; D020524:Thylakoids / Q000201:enzymology*
D045331:Photosystem I Protein Complex; D011994:Recombinant Proteins; D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases; D009601:Nitroreductases; D042967:Electron Transport Complex I