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	The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
	Marcia, Marco1; Ermler, Ulrich1; Peng, Guohong1,2; Michel, Hartmut1; Peng, GH, Max Planck Inst Biophys, Dept Mol Membrane Biol, Max von Laue Str 3, D-60438 Frankfurt, Germany
刊名	PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
	2009-06-16
卷号	106期号:24页码:9625-9630
关键词	Flavoprotein Monotopic Membrane Protein Sulfide Metabolism X-ray Crystallography Extremophilic Organism
ISSN号	0027-8424
DOI	10.1073/pnas.0904165106
文献子类	Article
英文摘要	Sulfide: quinone oxidoreductase (SQR) is a flavoprotein with homologues in all domains of life except plants. It plays a physiological role both in sulfide detoxification and in energy transduction. We isolated the protein from native membranes of the hyperthermophilic bacterium Aquifex aeolicus, and we determined its X-ray structure in the "as-purified,'' substrate-bound, and inhibitor-bound forms at resolutions of 2.3, 2.0, and 2.9 angstrom, respectively. The structure is composed of 2 Rossmann domains and 1 attachment domain, with an overall monomeric architecture typical of disulfide oxidoreductase flavoproteins. A. aeolicus SQR is a surprisingly trimeric, periplasmic integral monotopic membrane protein that inserts about 12 angstrom into the lipidic bilayer through an amphipathic helix-turn-helix tripodal motif. The quinone is located in a channel that extends from the si side of the FAD to the membrane. The quinone ring is sandwiched between the conserved amino acids Phe-385 and Ile-346, and it is possibly protonated upon reduction via Glu-318 and/or neighboring water molecules. Sulfide polymerization occurs on the re side of FAD, where the invariant Cys-156 and Cys-347 appear to be covalently bound to polysulfur fragments. The structure suggests that FAD is covalently linked to the polypeptide in an unusual way, via a disulfide bridge between the 8-methyl group and Cys-124. The applicability of this disulfide bridge for transferring electrons from sulfide to FAD, 2 mechanisms for sulfide polymerization and channeling of the substrate, S(2-), and of the product, S(n), in and out of the active site are discussed.; Sulfide: quinone oxidoreductase (SQR) is a flavoprotein with homologues in all domains of life except plants. It plays a physiological role both in sulfide detoxification and in energy transduction. We isolated the protein from native membranes of the hyperthermophilic bacterium Aquifex aeolicus, and we determined its X-ray structure in the "as-purified,'' substrate-bound, and inhibitor-bound forms at resolutions of 2.3, 2.0, and 2.9 angstrom, respectively. The structure is composed of 2 Rossmann domains and 1 attachment domain, with an overall monomeric architecture typical of disulfide oxidoreductase flavoproteins. A. aeolicus SQR is a surprisingly trimeric, periplasmic integral monotopic membrane protein that inserts about 12 angstrom into the lipidic bilayer through an amphipathic helix-turn-helix tripodal motif. The quinone is located in a channel that extends from the si side of the FAD to the membrane. The quinone ring is sandwiched between the conserved amino acids Phe-385 and Ile-346, and it is possibly protonated upon reduction via Glu-318 and/or neighboring water molecules. Sulfide polymerization occurs on the re side of FAD, where the invariant Cys-156 and Cys-347 appear to be covalently bound to polysulfur fragments. The structure suggests that FAD is covalently linked to the polypeptide in an unusual way, via a disulfide bridge between the 8-methyl group and Cys-124. The applicability of this disulfide bridge for transferring electrons from sulfide to FAD, 2 mechanisms for sulfide polymerization and channeling of the substrate, S2-, and of the product, S-n, in and out of the active site are discussed.
学科主题	Multidisciplinary Sciences
URL标识	查看原文
语种	英语
WOS记录号	WOS:000267045500017
公开日期	2010-11-18
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/1652]
专题	海洋研究所_实验海洋生物学重点实验室
通讯作者	Peng, GH, Max Planck Inst Biophys, Dept Mol Membrane Biol, Max von Laue Str 3, D-60438 Frankfurt, Germany
作者单位	1.Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany 2.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Marcia, Marco,Ermler, Ulrich,Peng, Guohong,et al. The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2009,106(24):9625-9630.
APA	Marcia, Marco,Ermler, Ulrich,Peng, Guohong,Michel, Hartmut,&Peng, GH, Max Planck Inst Biophys, Dept Mol Membrane Biol, Max von Laue Str 3, D-60438 Frankfurt, Germany.(2009).The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,106(24),9625-9630.
MLA	Marcia, Marco,et al."The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 106.24(2009):9625-9630.

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