Structural and Functional Insights into Sulfide:Quinone Oxidoreductase

被引：115

作者：

Brito, Jose A. ^{[1
]}

Sousa, Filipa L. ^{[1
]}

Stelter, Meike ^{[1
]}

Bandeiras, Tiago M. ^{[1
]}

Vonrhein, Clemens ^{[2
]}

Teixeira, Miguel ^{[1
]}

Pereira, Manuela M. ^{[1
]}

Archer, Margarida ^{[1
]}

机构：

[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2780157 Oeiras, Portugal

[2] Global Phasing Ltd, Cambridge CB3 0AX, England

来源：

BIOCHEMISTRY | 2009年 / 48卷 / 24期

关键词：

II NADH DEHYDROGENASE; QUINONE OXIDOREDUCTASE; ACIDIANUS-AMBIVALENS; HYDROGEN-SULFIDE; PROTEIN; OXIDATION; REDUCTASE; SULFUR; ENZYME; PURIFICATION;

D O I：

10.1021/bi9003827

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：

A sulfide:quinone oxidoreductase (SQR) was isolated from the membranes of the hyperthermoacidophilic archaeon Acidianus ambivalens, and its X-ray structure, the first reported for an SQR, was determined to 2.6 angstrom resolution. This enzyme was functionally and structurally characterized and was shown to have two redox active sites: a covalently bound FAD and an adjacent pair of cysteine residues. Most interestingly, the X-ray structure revealed the presence of a chain of three sulfur atoms bridging those two cysteine residues. The possible implications of this observation in the catalytic mechanism for sulfide oxidation are discussed, and the role of SQR in the sulfur dependent bioenergetics of A. ambivalens, linked to oxygen reduction, is addressed.

引用

页码：5613 / 5622

页数：10

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