| Role of NAD(P)H:quinone oxidoreductase encoded by drgA gene in reduction of exogenous quinones in cyanobacterium Synechocystis sp. PCC 6803 cells. | |
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MedLine Citation:
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PMID: 15000679 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Insertion mutant Ins2 of the cyanobacterium Synechocystis sp. PCC 6803, lacking NAD(P)H:quinone oxidoreductase (NQR) encoded by drgA gene, was characterized by higher sensitivity to quinone-type inhibitors (menadione and plumbagin) than wild type (WT) cells. In photoautotrophically grown cyanobacterial cells more than 60% of NADPH:quinone-reductase activity, as well as all NADPH:dinoseb-reductase activity, was associated with the function of NQR. NQR activity was observed only in soluble fraction of cyanobacterial cells, but not in membrane fraction. The effects of menadione and menadiol on the reduction of Photosystem I reaction center (P700(+)) after its photooxidation in the presence of DCMU were studied using the EPR spectroscopy. The addition of menadione increased the rate of P700(+) reduction in WT cells, whereas in Ins2 mutant the reduction of P700(+) was strongly inhibited. In the presence of menadiol the reduction of P700(+) was accelerated both in WT and Ins2 mutant cells. These data suggest that NQR protects the cyanobacterial cells from the toxic effect of exogenous quinones by their reduction to hydroquinones. These data may also indicate the probable functional homology of Synechocystis sp. PCC 6803 NQR with mammalian and plant NAD(P)H:quinone oxidoreductases (DT-diaphorases). |
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Authors:
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I V Elanskaya; V G Grivennikova; V V Groshev; G V Kuznetsova; M E Semina; K N Timofeev |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry. Biokhimii͡a Volume: 69 ISSN: 0006-2979 ISO Abbreviation: Biochemistry Mosc. Publication Date: 2004 Feb |
Date Detail:
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Created Date: 2004-03-05 Completed Date: 2005-01-19 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0376536 Medline TA: Biochemistry (Mosc) Country: United States |
Other Details:
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Languages: eng Pagination: 137-42 Citation Subset: IM |
Affiliation:
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Department of Genetics, Faculty of Biology, Lomonosov Moscow State University, Moscow 119992, Russia. ivelanskaya@mail.ru |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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genetics,
metabolism* Chlorophyll / metabolism* Cyanobacteria / enzymology*, genetics Drug Resistance, Bacterial / genetics Mutagenesis, Insertional NAD(P)H Dehydrogenase (Quinone) / genetics, metabolism* Oxidation-Reduction / drug effects Photosystem I Protein Complex / drug effects, metabolism Quinones / metabolism, pharmacology Vitamin K 3 / metabolism*, pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Photosystem I Protein Complex; 0/Quinones; 1406-65-1/Chlorophyll; 53321-11-2/chlorophyll P 700; 58-27-5/Vitamin K 3; EC 1.6.5.2/NAD(P)H Dehydrogenase (Quinone) |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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