Moore, Anthony L, Umbach, Ann L and Siedow, James N (1995) Strucute-Funtion-Relationships of the Alternative Oxidase of Plant-Mitochondria - A Model of the Active-Site. Journal of Bioenergetics and Biomembranes, 27 (4). pp. 367-377. ISSN 0145-479X

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Abstract

A major characteristic of plant mitochondria is the presence of a cyanide-insensitive alternative oxidase which catalyzes the reduction of oxygen to water. Current information on the properties of the oxidase is reviewed. Conserved amino acid motifs have been identified which suggest the presence of a hydroxo-bridged di-iron center in the active site of the alternative oxidase. On the basis of sequence comparison with other di-iron center proteins, a structural model for the active site of the alternative oxidase has been developed that has strong similarity to that of methane monoxygenase. Evidence is presented to suggest that the alternative oxidase of plant mitochondria is the newest member of the class II group of di-iron center proteins.

Item Type:	Article
Schools and Departments:	School of Life Sciences > Biochemistry
Depositing User:	Anthony Moore
Date Deposited:	06 Feb 2012 19:57
Last Modified:	22 Mar 2012 09:37
URI:	http://sro.sussex.ac.uk/id/eprint/23229

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