A revised model of the active site of alternative oxidase

FEBS Letters

Nordlund, Pär¹  Andersson, Martin E¹ 

[1] Department of Biochemistry, Stockholm University, S-106 91 Stockholm, Sweden

关键词: Alternative oxidase;    Fatty acid desaturase;    Plant mitochondrion;    Homology modeling;    Membrane protein;   

DOI  :  10.1016/S0014-5793(99)00376-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. A structure of this protein has previously been proposed based on an assumed structural homology to the di-iron carboxylate family of proteins. However, these authors suggested the protein has a very different topology than the known structures of di-iron carboxylate proteins. We have re-examined this model and based on comparison of recent sequences and structural data on di-iron carboxylate proteins we present a new model of the alternative oxidase which allows prediction of active site residues and a possible membrane binding motif.

【 授权许可】

Unknown