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

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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.

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Authors and Affiliations

  1. Department of Neurosurgery, The Methodist Hospital, 6565 Fannin Street, Houston, TX, 77030, USA

    Martyn A. Sharpe

  2. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824-1319, USA

    Shelagh Ferguson-Miller

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  1. Martyn A. Sharpe
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  2. Shelagh Ferguson-Miller
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Correspondence to Martyn A. Sharpe.

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Sharpe, M.A., Ferguson-Miller, S. A chemically explicit model for the mechanism of proton pumping in heme–copper oxidases. J Bioenerg Biomembr 40, 541–549 (2008). https://doi.org/10.1007/s10863-008-9182-6

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  • DOI: https://doi.org/10.1007/s10863-008-9182-6

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