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The intramitochondrial ATP/ADP‐ratio controls cytochrome c oxidase activity allosterically 1
Author(s) -
Arnold Susanne,
Kadenbach Bernhard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01694-9
Subject(s) - cytochrome c oxidase , oxidative phosphorylation , biochemistry , phosphorylation , cytochrome c , respiration , oxidase test , mitochondrion , chemistry , electron transport complex iv , cytochrome , signal transduction , enzyme , biology , anatomy
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.