Exploring the molecular nature of alternative oxidase regulation and catalysis

Affourtit, Charles, Albury, Mary S., Crichton, Paul G. ORCID: https://orcid.org/0000-0003-3786-8359 and Moore, Anthony L. (2002) Exploring the molecular nature of alternative oxidase regulation and catalysis. FEBS Letters, 510 (3). pp. 121-126. ISSN 0014-5793

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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.

Item Type:	Article
Uncontrolled Keywords:	alternative oxidase,ubiquinol-oxygen oxidoreductase,post-translational regulation,active site structure,catalytic mechanism,tyrosine radical,mmoh,hydroxylase component of methane monooxygenase,q, ubiquinone
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups:	Faculty of Medicine and Health Sciences > Research Groups > Cardiovascular and Metabolic Health Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	Pure Connector
Date Deposited:	03 Nov 2016 10:00
Last Modified:	19 Oct 2023 01:51
URI:	https://ueaeprints.uea.ac.uk/id/eprint/61211
DOI:	10.1016/S0014-5793(01)03261-6

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