Disulfide cross‐linking of subunits F1‐γ and F0I‐PVP(b) results in asymmetric effects on proton translocation in the mitochondrial ATP synthase

FEBS Letters

Gaballo, Antonio¹  Zanotti, Franco¹  Papa, Sergio¹  Raho, Gabriella¹ 

[1] Department of Medical Biochemistry and Biology, University of Bari, Piazza G. Cesare-Policlinico, 70125 Bari, Italy

关键词: H+-ATP synthase;    F0;    F1;    F0I-PVP(b) subunit;    F1-γ subunit;    H+ translocation;    FCCP;    carbonylcyanide p-(trifluoromethoxy)phenylhydrazone;    ESMP;    submitochondrial particles prepared in the presence of EDTA;    F0;    membrane integral sector of H+-ATP synthase;    F1;    catalytic sector of bovine heart H+-ATP synthase;    F1-γ;    protein subunit of mitochondrial F1;    F0I-PVP(b);    protein subunit of mitochondrial F0;    OSCP;    oligomycin sensitivity-conferring protein;    ACMA;    9-amino-6-chloro-2-methoxyacridine;    Neutral red;    3-amino-7-dimethylamino-2-methylphenazine hydrochloride;   

DOI  :  10.1016/S0014-5793(99)01593-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A study is presented on the effect of diamide-induced disulfide cross-linking of F₁-γ and F₀I-PVP(b) subunits on proton translocation in the mitochondrial ATP synthase. The results show that, upon cross-linking of these subunits, whilst proton translocation from the A side to the B F₁ side is markedly accelerated with decoupling of oxidative phosphorylation, proton translocation in the reverse direction, driven by either ATP hydrolysis or a diffusion potential, is unaffected. These observations reveal further peculiarities of the mechanism of energy transfer in the ATP synthase of coupling membranes.

【 授权许可】

Unknown