Exploring the molecular nature of alternative oxidase regulation and catalysis

Charles Affourtit, Mary S. Albury, Paul G. Crichton, Anthony L. Moore

Research output: Contribution to journalArticle

108 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)121-126
Number of pages6
JournalFEBS Letters
Volume510
Issue number3
Early online date11 Dec 2001
DOIs
Publication statusPublished - 16 Jan 2002

Keywords

  • Alternative oxidase
  • Ubiquinol-oxygen oxidoreductase
  • Post-translational regulation
  • Active site structure
  • Catalytic mechanism
  • Tyrosine radical
  • MMOH
  • hydroxylase component of methane monooxygenase
  • Q, ubiquinone

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