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

被引：116

作者：

Arnold, S ^{[1
]}

Kadenbach, B ^{[1
]}

机构：

[1] Univ Marburg, Fachbereich Chem, D-35032 Marburg, Germany

来源：

FEBS LETTERS | 1999年 / 443卷 / 02期

关键词：

cytochrome c oxidase; respiratory control; nucleotide binding; allosteric effector; ATP/ADP ratio;

D O I：

10.1016/S0014-5793(98)01694-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recently the signal transduction function for oxidative phosphorylation mns 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. (C) 1999 Federation of European Biochemical Societies.

引用

页码：105 / 108

页数：4

共 26 条

[1]

[Anonymous], 1997, FRONTIERS METABOLISM

[2] TISSUE-SPECIFIC REGULATION OF BOVINE HEART CYTOCHROME-C-OXIDASE ACTIVITY BY ADP VIA INTERACTION WITH SUBUNIT-VIA [J].