Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite

Jaume Torres, Martyn A. Sharpe, Aasa Rosquist, Chris E. Cooper, Mike T. Wilson

Research output: Contribution to journalArticlepeer-review

102 Scopus citations


Previous studies have shown that the addition of nitric oxide to cytochrome c oxidase rapidly generates spectral changes compatible with the formation of nitrite at the binuclear haem:copper centre. Here we directly demonstrate nitrite release following nitric oxide addition to the enzyme. The nitrite complex is kinetically inactive and the off rate for nitrite was found to be slow (0.024 min-1). However, the presence of reductants enhances the off rate and enables cytochrome oxidase to catalyse the rapid oxidation of nitric oxide to nitrite free in solution. This may play a major role in the mitochondrial metabolism of nitric oxide. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)263-266
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - Jun 23 2000


  • Cytochrome c
  • Cytochrome c oxidase
  • Inhibition
  • Metabolism
  • Nitric oxide
  • Nitrite

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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