The alternative oxidases: simple oxidoreductase proteins with complex functions

Author:

Young Luke1,Shiba Tomoo2,Harada Shigeharu2,Kita Kiyoshi3,Albury Mary S.1,Moore Anthony L.1

Affiliation:

1. Department of Biochemistry and Molecular Biology, School of Life Sciences, University of Sussex, Brighton BN1 9QG, U.K.

2. Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto 606-8585, Japan

3. Department of Biomedical Chemistry, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan

Abstract

The alternative oxidases are membrane-bound monotopic terminal electron transport proteins found in all plants and in some agrochemically important fungi and parasites including Trypansoma brucei, which is the causative agent of trypanosomiasis. They are integral membrane proteins and reduce oxygen to water in a four electron process. The recent elucidation of the crystal structure of the trypanosomal alternative oxidase at 2.85 Å (1 Å=0.1 nm) has revealed salient structural features necessary for its function. In the present review we compare the primary and secondary ligation spheres of the alternative oxidases with other di-iron carboxylate proteins and propose a mechanism for the reduction of oxygen to water.

Publisher

Portland Press Ltd.

Subject

Biochemistry

Reference36 articles.

1. Unraveling the heater: new insights into the structure of the alternative oxidase;Moore;Annu. Rev. Plant Biol.,2013

2. Origins, evolutionary history, and taxonomic distribution of alternative oxidase and plastoquinol terminal oxidase;McDonald;Comp. Biochem. Physiol., Part D: Genomics Proteomics,2006

3. Biochemical and molecular properties of the Trypanosoma brucei alternative oxidase;Chaudhuri;Mol. Biochem. Parasitol.,1998

4. Trypanosome alternative oxidase: from molecule to function;Chaudhuri;Trends Parasitol.,2006

5. Evidence for mitochondrial-derived alternative oxidase in the apicomplexan parasite Cryptosporidium parvum: a potential anti-microbial agent target;Roberts;Int. J. Parasitol.,2004

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