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Towards a structural elucidation of the alternative oxidase in plants

Authors

  • Mary S. Albury,

    1. Division of Biochemistry and Biomedical Sciences, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, UK
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  • Catherine Elliott,

    1. Division of Biochemistry and Biomedical Sciences, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, UK
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  • Anthony L. Moore

    Corresponding author
    1. Division of Biochemistry and Biomedical Sciences, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, UK
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e-mail: a.l.moore@sussex.ac.uk

Abstract

In addition to the conventional cytochrome c oxidase, mitochondria of all plants studied to date contain a second cyanide-resistant terminal oxidase or alternative oxidase (AOX). The AOX is located in the inner mitochondrial membrane and branches from the cytochrome pathway at the level of the quinone pool. It is non-protonmotive and couples the oxidation of ubiquinone to the reduction of oxygen to water. For many years, the AOX was considered to be confined to plants, fungi and a small number of protists. Recently, it has become apparent that the AOX occurs in wide range of organisms including prokaryotes and a moderate number of animal species. In this paper, we provide an overview of general features and current knowledge available about the AOX with emphasis on structure, the active site and quinone-binding site. Characterisation of the AOX has advanced considerably over recent years with information emerging about the role of the protein, regulatory regions and functional sites. The large number of sequences available is now enabling us to obtain a clearer picture of evolutionary origins and diversity.

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