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

FEBS Lett. 1999 Jan 25;443(2):105-8. doi: 10.1016/s0014-5793(98)01694-9.


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, 27995-279981, 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism*
  • Adenosine Triphosphate / metabolism*
  • Allosteric Regulation
  • Animals
  • Ascorbic Acid / metabolism
  • Cattle
  • Electron Transport Complex IV / metabolism*
  • Kinetics
  • Mitochondria, Heart / metabolism*


  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Electron Transport Complex IV
  • Ascorbic Acid