Structures of the intermediates in the catalytic cycle of mitochondrial cytochrome c oxidase

Mårten Wikström, Robert B. Gennis, Peter R. Rich

Research output: Contribution to journalReview articlepeer-review


Cytochrome c oxidase is the terminal complex of the respiratory chains in the mitochondria of nearly all eukaryotes. It catalyzes the reduction of molecular O2 to water using electrons from the respiratory chain, delivered via cytochrome c on the external surface of the inner mitochondrial membrane. The protons required for water formation are taken from the matrix side of the membrane, making catalysis vectorial. This vectorial feature is further enhanced by the fact that the redox catalysis is coupled to the translocation of protons from the inside to the outside of the inner mitochondrial membrane. We are dealing with a molecular machine that converts redox free energy into a protonmotive force (pmf). Here, we review the current extensive knowledge of the structural changes in the active heme‑copper site that accompany catalysis, based on a large variety of time-resolved spectroscopic experiments, X-ray and cryoEM structures, and advanced computational chemistry.

Original languageEnglish (US)
Article number148933
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number2
StatePublished - Apr 1 2023


  • Cell respiration
  • Heme‑copper oxidases
  • Oxygen reduction
  • Respiratory chain

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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