Journal
FEBS LETTERS
Volume 510, Issue 3, Pages 121-126Publisher
WILEY
DOI: 10.1016/S0014-5793(01)03261-6
Keywords
alternative oxidase; ubiquinol-oxygen oxidoreductase; post-translational regulation; active site structure; catalytic mechanism; tyrosine radical
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Plant mitochondria contain a non-protonmotive alternative oxidase (AOX) that couples the oxidation of ubiquinol to the complete reduction of oxygen to water. In this paper we review theoretical and experimental studies that have contributed to our current structural and mechanistic understanding of the oxidase and to the clarification of the molecular nature of post-translational regulatory phenomena. Furthermore, we suggest a catalytic cycle for AOX that involves at least one transient protein-derived radical. The model is based on the reviewed information and on recent insights into the mechanisms of cytochrome c oxidase and the hydroxylase component of methane monooxygenase. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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