Journal of Bioenergetics and Biomembranes

, Volume 40, Issue 5, pp 541–549

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

Article

DOI: 10.1007/s10863-008-9182-6

Cite this article as:
Sharpe, M.A. & Ferguson-Miller, S. J Bioenerg Biomembr (2008) 40: 541. doi:10.1007/s10863-008-9182-6

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.

Keywords

Proton pumping Heme–copper oxidases Chemiosmotic principles 

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  1. 1.Department of NeurosurgeryThe Methodist HospitalHoustonUSA
  2. 2.Department of Biochemistry and Molecular BiologyMichigan State UniversityEast LansingUSA

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