Molecular mechanism of energy conservation in polysulfide respiration

被引：135

作者：

Jormakka, Mika ^{[1
,2
,3
]}

Yokoyama, Ken ^{[4
,5
]}

Yano, Takahiro ^{[5
]}

Tamakoshi, Masatada ^{[6
]}

Akimoto, Satoru ^{[5
]}

Shimamura, Tatsuro ^{[7
,8
]}

Curmi, Paul ^{[1
]}

Iwata, So ^{[8
,9
,10
]}

机构：

[1] Univ New S Wales, Dept Biophys, Sydney, NSW 2052, Australia

[2] Univ Sydney, Centenary Inst Canc Med & Cell Biol, Struct Biol Program, Sydney, NSW 2042, Australia

[3] Univ Sydney, Fac Med, Cent Clin Sch, Sydney, NSW 2006, Australia

[4] Tokyo Inst Technol, Chem Resources Lab, Midori Ku, Yokohama, Kanagawa 2268503, Japan

[5] Japan Sci & Technol Agcy, ICORP ATP Synth Regulat Project, Koto Ku, Tokyo 1350064, Japan

[6] Tokyo Univ Pharm & Life Sci, Dept Biol Mol, Tokyo 1920392, Japan

[7] RIKEN SPring 8 Ctr, Struct Biophys Lab, Sayo, Hyogo 6795148, Japan

[8] Japan Sci & Technol Agcy, ERATO, Human Crystallog Project, Sakyo Ku, Kyoto 606851, Japan

[9] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, Membrane Prot Crystallog Grp, London SW7 2AZ, England

[10] RIKEN Genom Sci Ctr, Yokohama, Kanagawa 2300045, Japan

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 07期

基金：

英国惠康基金;

关键词：

D O I：

10.1038/nsmb.1434

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：

Bacterial polysulfide reductase (PsrABC) is an integral membrane protein complex responsible for quinone-coupled reduction of polysulfide, a process important in extreme environments such as deep-sea vents and hot springs. We determined the structure of polysulfide reductase from Thermus thermophilus at 2.4-angstrom resolution, revealing how the PsrA subunit recognizes and reduces its unique polyanionic substrate. The integral membrane subunit PsrC was characterized using the natural substrate menaquinone-7 and inhibitors, providing a comprehensive representation of a quinone binding site and revealing the presence of a water-filled cavity connecting the quinone binding site on the periplasmic side to the cytoplasm. These results suggest that polysulfide reductase could be a key energy-conserving enzyme of the T. thermophilus respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane via a previously unknown mechanism.

引用

页码：730 / 737

页数：8

共 59 条

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