Hydrogen peroxide is not released following reaction of cyanide with several catalytically important derivatives of cytochrome c oxidase

FEBS Lett. 1998 Jan 23;422(1):1-4. doi: 10.1016/s0014-5793(97)01561-5.

Abstract

We have looked for the production of hydrogen peroxide following reaction of oxidized cytochrome c oxidase and two oxy derivatives (compounds P and F) with cyanide. In each case the final product was the cyanide adduct of cytochrome c oxidase. In no case release of hydrogen peroxide was detected, as gauged by the scopoletin plus horse radish peroxidase assay. The simplest conclusion is that none of these forms of the enzyme contains intact hydrogen peroxide.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cyanides / metabolism*
  • Electron Transport Complex IV / metabolism*
  • Fluorescence
  • Hemeproteins / metabolism
  • Horseradish Peroxidase / metabolism
  • Hydrogen Peroxide / metabolism*
  • Kinetics
  • Scopoletin / metabolism
  • Spectrophotometry

Substances

  • Cyanides
  • Hemeproteins
  • Hydrogen Peroxide
  • Horseradish Peroxidase
  • Electron Transport Complex IV
  • Scopoletin