F0F1‐ATPase from Vibrio alginolyticus Subunit composition and proton pumping activity

FEBS Letters

Dmitriev, O.Yu.²  Krasnoselskaya, I.A.²  Papa, S.¹  Skulachev, V.P.² 

[1]Institute of Medical Biochemistry and Chemistry, University of Bari, Bari, Italy

[2]A.N. Belozersky Laboratory for Molecular Biology and Bioorganic Chemistry, Moscow State University, 119899, Moscow, USSR

关键词: F0F1-ATPase;    H+ pump;    Proteoliposome. Vibrio alginolyticus;    DCCD;    N;    N′-dicyclohexylcarbodiimide;    FCCP;    carbonylcyanide-4-trifluormethoxyphenylhydrazone;    DTT;    dithlotreitol;   

DOI  :  10.1016/0014-5793(91)80702-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An F₀F₁-ATPase was isolated from the membranes of the marine bacterium Vibrio alginolyticus. Homology between the subunits of the F₀-complexes from E. coli and V. alginolyticus was found using antibodies against subunits a, b and c of the E. coli F₀F₁-ATPase. The F₀F₁-complex from V. alginolyticus was reconstituted into proteoliposomes, which were competent in ATP-dependent proton uptake. This process was inhibited by triphenyltin, DCCD, and venturicidin. Na⁺ did not affect proton translocation.

【 授权许可】

Unknown