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Mechanism of Proton-Motive Activity of Heme-Copper Oxidases

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Frontiers of Cellular Bioenergetics

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Abstract

Mammalian mitochondrial cytochrome c oxidase is responsible for the terminal step in the respiratory electron transfer chain of oxidation of cytochrome c and reduction of molecular oxygen. Energy from these reactions is conserved both because of the vectorial nature of the redox reactions and because of an associated mechanism that results in translocation of additional protons across the membrane. It has become clear that the mammalian enzyme is one member of a large and diverse superfamily of homologous oxidases that is widely distributed and includes both cytochrome c and quinol-oxidizing forms (Saraste et al., 1991). The influences of molecular biology and successes in solving two oxidase structures to atomic resolution (Tsukihara et al., 1995, 1996; Iwata et al., 1995) have clarified many issues and allow consideration of mechanistic questions at the atomic level. Of particular interest is the way in which electron transfer and oxygen reduction chemistry are coupled to the processes that result in the net transfer of protons across the membrane and the conservation of energy for subsequent use in endergonic processes such as ATP synthesis. The purpose of the present chapter is to review recent ideas on some of the critical features that likely underlie the mechanism of coupling of proton and electron transfers and to relate them to the available structural information.

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Authors and Affiliations

  1. Department of Biology, University College, London, WC1E 6BT, England

    Peter R. Rich

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  1. Peter R. Rich
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Editors and Affiliations

  1. University of Bari, Bari, Italy

    Sergio Papa  & Ferruccio Guerrieri  & 

  2. University of Amsterdam, Amsterdam, The Netherlands

    Joseph M. Tager

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Rich, P.R. (1999). Mechanism of Proton-Motive Activity of Heme-Copper Oxidases. In: Papa, S., Guerrieri, F., Tager, J.M. (eds) Frontiers of Cellular Bioenergetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4843-0_8

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  • DOI: https://doi.org/10.1007/978-1-4615-4843-0_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7196-0

  • Online ISBN: 978-1-4615-4843-0

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