A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases

Martyn A. Sharpe, Shelagh Ferguson-Miller

Research output: Contribution to journalReview article

57 Scopus citations

Abstract

A mechanism for proton pumping is described that is based on chemiosmotic principles and the detailed molecular structures now available for cytochrome oxidases. The importance of conserved water positions and a step-wise gated process of proton translocation is emphasized, where discrete electron transfer events are coupled to proton uptake and expulsion. The trajectory of each pumped proton is the same for all four substrate electrons. An essential role for the His-Tyr cross-linked species is discussed, in gating of the D- and K-channels and as an acceptor/donor of electrons and protons at the binuclear center.

Original languageEnglish (US)
Pages (from-to)541-549
Number of pages9
JournalJournal of Bioenergetics and Biomembranes
Volume40
Issue number5
DOIs
StatePublished - Oct 2008

Keywords

  • Chemiosmotic principles
  • Heme-copper oxidases
  • Proton pumping

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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