FEBS Letters | |
The Na+/e− stoichiometry of the Na+‐motive NADH : quinone oxidoreductase in Vibrio alginolyticus | |
Murtazina, Rachilya A1  Bogachev, Alexander V1  Skulachev, Vladimir P1  | |
[1] Department of Bioenergetics, A.N. Belozersky Institute of Physico–Chemical Biology, Moscow State University, Moscow 119899, Russia | |
关键词: Na+/e− stoichiometry; Na+-motive NADH : quinone oxidoreductase; Vibrio alginolyticus; and; transmembrane differences in H+ and Na+ electrochemical potentials; respectively; ΔΨ; transmembrane difference in electric potentials; CCCP; m-chlorocarbonylcyanide phenylhydrazone; HQNO; 2-heptyl-4-hydrooxyquinoline N-oxide; TPP+; tetraphenyl phosphonium; TTFB; 4; 5; 6; 7-tetra-chloro-2-trifluoromethylbenzimidazole; | |
DOI : 10.1016/S0014-5793(97)00536-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
A method is proposed to estimate the stoichiometries of primary Na+-pumps in intact bacterial cells. It is based on technique when the H+/e− stoichiometry is measured in the presence of protophorous uncoupler and in the absence of penetrating ions other than H+. Under these conditions, the H+ influx discharges membrane potential generated by the Na+ pump so the Na+/e− and H+/e− ratios become equal. Using this approach it is shown that the Na+/e− ratio for the Na+-motive NADH : quinone oxidoreductase of Vibrio alginolyticus is equal to 0.71±0.06. The Na+/e− stoichiometry appears to be ≈1, provided that the contribution of the non-coupled NADH : quinone oxidoreductase, which is resistant to low HQNO concentrations, is taken into account.
【 授权许可】
Unknown
【 预 览 】
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