Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors
文献类型：期刊论文
| 作者 | Gao, Ye1; Meyer, Bjoern2; Sokolova, Lucie3; Zwicker, Klaus4; Karas, Michael2; Brutschy, Bernd3; Peng, Guohong1,5; Michel, Hartmut1 |
| 刊名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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| 出版日期 | 2012-02-28 |
| 卷号 | 109期号:9页码:3275-3280 |
| 关键词 | cytochrome c oxidase quinol oxidase cyanide inhibition protein complex interaction |
| ISSN号 | 0027-8424 |
| 通讯作者 | Peng, GH (reprint author), Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany. |
| 英文摘要 | 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. |
| 学科主题 | Multidisciplinary Sciences |
| 收录类别 | SCI |
| 原文出处 | 10.1073/pnas.1121040109 |
| 语种 | 英语 |
| WOS记录号 | WOS:000300828200024 |
| 公开日期 | 2013-09-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/12339]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 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.,...&Michel, Hartmut.(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. |
入库方式： OAI收割
来源：海洋研究所
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