Catalytic and activating protons follow different pathways in the H+‐ATPase of potato tuber mitochondria

FEBS Letters

Valerio, Marie¹  Haraux, Francis¹ 

[1] Biosystèmes Membranaires (ERS 30), CNRS, 91198 Gif-sur-Yvette, France

关键词: F0F1 H+-ATPase;    Electrochemical proton gradient;    Enzyme activation;    Inhibitor;    Lauryldimethylamine oxide;    Plant mitochondria;    F0 and F1;    membranous and extrinsic parts of the proton ATPase;    IF1;    inhibitory peptide of the mitochondrial ATPase;    Δ/̃gm-H+;    transmembrane difference in electrochemical proton potential;    Δϕ;    trans-membrane potential difference;    TPP+;    tetraphenylphosphonium;    LDAO;    lauryldimethylamine oxide;    VTCD;    venturicidin;    TNBT;    tri-n-butyltin;   

DOI  :  10.1016/0014-5793(93)81614-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of some F₀F₁ inhibitors on the activation of the H⁺-ATPase by the electrochemical proton gradient was investigated in mitochondria extracted from potato tubers. Transient activated state of the ATPase was revealed by addition of ATP and of the detergent lauryldimethylamine oxide (LDAO) to energized mitochondria. Venturicidin, tri-n-butyltin and aurovertin at high concentrations did not affect the process of Δ/̃gm_H⁺-activation, whereas oligomycin fully blocked it. The results support the idea of separate pathways or binding sites for catalytic and activating protons.

【 授权许可】

Unknown