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Exploring the molecular nature of alternative oxidase regulation and catalysis
Author(s) -
Affourtit Charles,
Albury Mary S,
Crichton Paul G,
Moore Anthony L
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03261-6
Subject(s) - alternative oxidase , chemistry , monooxygenase , cytochrome c oxidase , oxidase test , catalytic cycle , biochemistry , ubiquinol , mitochondrion , enzyme , biophysics , cytochrome p450 , biology , cytochrome c , coenzyme q – cytochrome c reductase
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.