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FAD and FMN flavoproteins participate in the sodium‐transport respiratory chain NADH:quinone reductase of a marine bacterium, Vibrio alginolyticus
Author(s) -
Hayashi Maki,
Unemoto Tsutomu
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80711-6
Subject(s) - nadh dehydrogenase , quinone , reductase , respiratory chain , biochemistry , flavoprotein , vibrio alginolyticus , chemistry , ubiquinol , protein subunit , stereochemistry , bacteria , biology , vibrio , enzyme , coenzyme q – cytochrome c reductase , cytochrome c , mitochondrion , genetics , gene
The sodium‐transport respiratory chain NADH:quinone reductase of a marine bacterium, Vibrio alginolyti‐cus , is composed of three protein subunits, α,β and γ. The β‐subunit contains FAD as a prosthetic group and corresponds to NADH dehydrogenase, which catalyses the reduction of ubiquinone to ubisemiquinone. In addition to β, subunits α. and γ are essential for the quinone reductase, which catalyses the reduction of ubiquinone to ubiquinol. The α‐subunit contains FMN and the reaction catalysed by subunit α is related to the coupling site of the sodium pump in the quinone reductase.