Transmembrane proton translocation by cytochrome c oxidase

Gisela Brändén, Robert B. Gennis, Peter Brzezinski

Research output: Contribution to journalReview article

Abstract

Respiratory heme-copper oxidases are integral membrane proteins that catalyze the reduction of molecular oxygen to water using electrons donated by either quinol (quinol oxidases) or cytochrome c (cytochrome c oxidases, CcOs). Even though the X-ray crystal structures of several heme-copper oxidases and results from functional studies have provided significant insights into the mechanisms of O2-reduction and, electron and proton transfer, the design of the proton-pumping machinery is not known. Here, we summarize the current knowledge on the identity of the structural elements involved in proton transfer in CcO. Furthermore, we discuss the order and timing of electron-transfer reactions in CcO during O2 reduction and how these reactions might be energetically coupled to proton pumping across the membrane.

Original languageEnglish (US)
Pages (from-to)1052-1063
Number of pages12
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1757
Issue number8
DOIs
StatePublished - Aug 1 2006

Keywords

  • Cytochrome aa
  • Electrochemical proton gradient
  • Electron transfer
  • Proton transfer
  • Quinol oxidase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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