The intramitochondrial ATP/ADP‐ratio controls cytochrome c oxidase activity allosterically 1

FEBS Letters

Arnold, Susanne¹  Kadenbach, Bernhard¹ 

[1] Fachbereich Chemie, Philipps-Universität, D-35032 Marburg, Germany

关键词: Cytochrome c oxidase;    Respiratory control;    Nucleotide binding;    Allosteric effector;    ATP/ADP ratio;    PEP;    phosphoenolpyruvate;    PK;    pyruvate kinase;    CCCP;    carbonylcyanide-m-chlorophenylhydrazone;    ΔΨ;    mitochondrial membrane potential;    Δp;    proton motive force;   

DOI  :  10.1016/S0014-5793(98)01694-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recently the signal transduction function for oxidative phosphorylation was found to be second order in ADP [Jeneson, J.A.L., Wiseman, R.W., Westerhoff, H.V. and Kushmerick, M.J. (1996) J. Biol. Chem. 271, 27995–27998], but the molecular mechanism of signal transduction remained unclear. Previously we described inhibition of cytochrome c oxidase by intramitochondrial ATP, accompanied by a change of hyperbolic into sigmoidal kinetics. The present study describes a sigmoidal relationship also between the ascorbate respiration of reconstituted cytochrome c oxidase and intraliposomal ADP concentration. Its possible role in the control of oxidative phosphorylation and cell respiration is discussed.

【 授权许可】

Unknown