Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors

doi:10.1073/pnas.1121040109

IOCAS-IR > 实验海洋生物学重点实验室

	Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors
	Gao, Ye 1; Meyer, Bjoern 2; Sokolova, Lucie 3; Zwicker, Klaus 4; Karas, Michael 2; Brutschy, Bernd 3; Peng, Guohong 1,5; Michel, Hartmut 1; Peng, GH (reprint author), Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany.
	2012-02-28
发表期刊	PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN	0027-8424
卷号	109 期号:9 页码:3275-3280
文章类型	Article
摘要	The cytochrome c oxidase Cox2 has been purified from native membranes of the hyperthermophilic eubacterium Aquifex aeolicus. It is a cytochrome ba(3) oxidase belonging to the family B of the heme-copper containing terminal oxidases. It consists of three subunits, subunit I (CoxA2, 63.9 kDa), subunit II (CoxB2, 16.8 kDa), and an additional subunit IIa of 5.2 kDa. Surprisingly it is able to oxidize both reduced cytochrome c and ubiquinol in a cyanide sensitive manner. Cox2 is part of a respiratory chain supercomplex. This supercomplex contains the fully assembled cytochrome bc(1) complex and Cox2. Although direct ubiquinol oxidation by Cox2 conserves less energy than ubiquinol oxidation by the cytochrome bc(1) complex followed by cytochrome c oxidation by a cytochrome c oxidase, ubiquinol oxidation by Cox2 is of advantage when all ubiquinone would be completely reduced to ubiquinol, e.g., by the sulfide: quinone oxidoreductase, because the cytochrome bc(1) complex requires the presence of ubiquinone to function according to the Q-cycle mechanism. In the case that all ubiquinone has been reduced to ubiquinol its reoxidation by Cox2 will enable the cytochrome bc(1) complex to resume working.
关键词	Cytochrome c Oxidase Quinol Oxidase Cyanide Inhibition Protein Complex Interaction
学科领域	Multidisciplinary Sciences
DOI	10.1073/pnas.1121040109
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000300828200024
引用统计	被引频次：25[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/12339
专题	实验海洋生物学重点实验室
通讯作者	Peng, GH (reprint author), Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany.
作者单位	1.Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany 2.Goethe Univ Frankfurt, Inst Pharmaceut Chem, D-60438 Frankfurt, Germany 3.Goethe Univ Frankfurt, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany 4.Goethe Univ Frankfurt, Sch Med, D-60590 Frankfurt, Germany 5.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Gao, Ye,Meyer, Bjoern,Sokolova, Lucie,et al. Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2012,109(9):3275-3280.
APA	Gao, Ye.,Meyer, Bjoern.,Sokolova, Lucie.,Zwicker, Klaus.,Karas, Michael.,...&Peng, GH .(2012).Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,109(9),3275-3280.
MLA	Gao, Ye,et al."Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 109.9(2012):3275-3280.

条目包含的文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
Heme-copper terminal（989KB）			限制开放	使用许可	浏览