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On the Mechanism of Proton Translocation by Respiratory Enzyme

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Abstract

The protonmotive function of the respiratory heme-copper oxidases is often described as the sum of two separate mechanisms: a proton pump plus an incomplete Mitchellian redox loop. However, these two functions may be mechanistically intertwined so that the uptake of protons to form water during the reduction of O2 is a crucial part of the proton pump mechanism itself. This principle can be deduced from thermodynamic, kinetic, mechanistic, as well as from structural considerations, and was first proposed in conjunction with a histidine cycle model of proton translocation [Morgan, J. E., Verkhovsky, M. I., and Wikström, M. (1994). J. Bioenerg. Biomembr. 26, 599–608]. However, histidine cycle models go much further to suggest chemical details of how this principle might be applied.

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Authors and Affiliations

  1. Helsinki Bioenergetics Group, Department of Medical Chemistry, Institute of Biomedical Sciences, and Biocentrum Helsinki, University of Helsinki, P. O. Box 8, 00014, Helsinki, Finland

    Mårten Wikström, Joel E. Morgan & Michael I. Verkhovsky

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  1. Mårten Wikström
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  2. Joel E. Morgan
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  3. Michael I. Verkhovsky
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Wikström, M., Morgan, J.E. & Verkhovsky, M.I. On the Mechanism of Proton Translocation by Respiratory Enzyme. J Bioenerg Biomembr 30, 139–145 (1998). https://doi.org/10.1023/A:1020576031758

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