A structural model for the membrane-integral domain of succinate:quinone oxidoreductases

被引：114

作者：

Hagerhall, C ^{[1
]}

Hederstedt, L ^{[1
]}

机构：

[1] LUND UNIV, DEPT MICROBIOL, S-22362 LUND, SWEDEN

来源：

FEBS LETTERS | 1996年 / 389卷 / 01期

关键词：

succinate dehydrogenase; fumarate reductase; cytochrome b; heme protein; quinone reductase;

D O I：

10.1016/0014-5793(96)00529-7

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：

Many succinate:quinone oxidoreductases in bacteria and mitochondria, i.e, succinate:quinone reductases and fumarate reductases, contain in the membrane anchor a cytochrome b whose structure and function is poorly understood, Based on biochemical data and polypeptide sequence information, we show that the anchors in different organisms are related despite an apparent diversity in polypeptide and heme composition, A general structural model for the membrane-integral domain of the anchors is proposed, It is an antiparallel four-helix bundle with a novel arrangement of hexa-coordinated protoheme M. The structure can be applied to a larger group of membrane-integral cytochromes of b-type and has evolutionary and functional implications.

引用

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页码：25 / 31

页数：7

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