Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP

Biochem Mol Biol Int. 1998 Aug;45(5):1047-55. doi: 10.1002/iub.7510450522.

Abstract

The activity of reconstituted cytochrome c oxidase from bovine heart but not from Rhodobacter sphaeroides is allosterically inhibited by intraliposomal ATP, which binds to subunit IV. The activity of cytochrome c oxidase of wild-type yeast and of a subunit VIa-deleted yeast mutant, measured with Tween 20-solubilized mitochondria in the presence of an ATP-regenerating system, was also allosterically inhibited by ATP, indicating the general validity of this mechanism of "respiratory control" in eucaryotic cytochrome c oxidases (Arnold and Kadenbach, Eur. J. Biochem. (1997) 249, 350-354). Deletion of subunit VIa changes the biphysic into monophysic kinetics of the yeast enzyme in the presence of ADP. A tenfold higher amount of horse heart cytochrome c, as compared to yeast cytochrome c, was required to relieve the ATP inhibition of the yeast enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Diphosphate / pharmacology
  • Adenosine Triphosphate / metabolism
  • Adenosine Triphosphate / pharmacology*
  • Allosteric Regulation
  • Animals
  • Binding Sites
  • Cattle
  • Electron Transport Complex IV / antagonists & inhibitors*
  • Electron Transport Complex IV / genetics
  • Electron Transport Complex IV / metabolism
  • Kinetics
  • Mitochondria / enzymology
  • Mitochondria, Heart / enzymology*
  • Mutation
  • Rhodobacter sphaeroides / enzymology*
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Electron Transport Complex IV