A revised model of the active site of alternative oxidase

被引：122

作者：

Andersson, ME ^{[1
]}

Nordlund, P ^{[1
]}

机构：

[1] Univ Stockholm, Dept Biochem, S-10691 Stockholm, Sweden

来源：

FEBS LETTERS | 1999年 / 449卷 / 01期

关键词：

alternative oxidase; fatty acid desaturase; plant mitochondrion; homology modeling; membrane protein;

D O I：

10.1016/S0014-5793(99)00376-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 reexamined 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. (C) 1999 Federation of European Biochemical Societies.

引用

页码：17 / 22

页数：6

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