Current issues in the chemistry of cytochrome c oxidase

J Bioenerg Biomembr. 1993 Apr;25(2):145-51. doi: 10.1007/BF00762856.


Some contemporary issues relevant to the chemistry of mammalian cytochrome c oxidase are discussed. These include the optical properties of heme A and the spectroscopic consequences of the differences in side-chain substitution compared to heme B; a common fallacy concerning the electrostatic exchange interaction between cytochrome a3 and CuB; the question of the number and location of the copper components of the enzyme; and the mode of binding of ligands such as cyanide and azide.

Publication types

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

MeSH terms

  • Animals
  • Azides / metabolism
  • Azides / pharmacology
  • Binding Sites
  • Copper / analysis
  • Cyanides / metabolism
  • Cyanides / pharmacology
  • Electron Transport Complex IV / chemistry*
  • Electron Transport Complex IV / isolation & purification
  • Electron Transport Complex IV / metabolism
  • Heme / chemistry
  • Heme / metabolism
  • Mammals
  • Oxidation-Reduction
  • Sodium Azide


  • Azides
  • Cyanides
  • Heme
  • Copper
  • Sodium Azide
  • Electron Transport Complex IV