气候变化领域集成服务门户(CCPortal): A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria

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DOI	10.1073/pnas.2001572117
	A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria
	Maréchal A.; Xu J.-Y.; Genko N.; Hartley A.M.; Haraux F.; Meunier B.; Rich P.R.
发表日期	2020
ISSN	0027-8424
起始页码	9349
结束页码	9355
卷号	117 期号:17
英文摘要	Mitochondria metabolize almost all the oxygen that we consume, reducing it to water by cytochrome c oxidase (CcO). CcO maximizes energy capture into the protonmotive force by pumping protons across the mitochondrial inner membrane. Forty years after the H+/e− stoichiometry was established, a consensus has yet to be reached on the route taken by pumped protons to traverse CcO’s hydrophobic core and on whether bacterial and mitochondrial CcOs operate via the same coupling mechanism. To resolve this, we exploited the unique amenability to mitochondrial DNA mutagenesis of the yeast Saccharomyces cerevisiae to introduce single point mutations in the hydrophilic pathways of CcO to test function. From adenosine diphosphate to oxygen ratio measurements on preparations of intact mitochondria, we definitely established that the D-channel, and not the H-channel, is the proton pump of the yeast mitochondrial enzyme, supporting an identical coupling mechanism in all forms of the enzyme. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	ADP/O ratio; Cytochrome c oxidase; H/e stoichiometry; Mitochondria; Proton pumping
语种	英语
scopus关键词	adenosine diphosphate; cytochrome c oxidase; heme copper oxidase; mitochondrial DNA; oxidoreductase; unclassified drug; copper; copper oxidase; cytochrome c oxidase; heme; oxidoreductase; oxygen; proton; proton pump; Saccharomyces cerevisiae protein; Article; bacterium; catalysis; controlled study; coupling factor; crystal structure; enzyme metabolism; gene mutation; hydrophilicity; hydrophobicity; mitochondrion; mutagenesis; nonhuman; point mutation; priority journal; Saccharomyces cerevisiae; sequence homology; signal transduction; bacterium; chemistry; genetics; ion transport; metabolism; mitochondrial membrane; mitochondrion; oxidation reduction reaction; Bacteria; Copper; Electron Transport Complex IV; Heme; Ion Transport; Mitochondria; Mitochondrial Membranes; Oxidation-Reduction; Oxidoreductases; Oxygen; Proton Pumps; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160298
作者单位	Maréchal, A., Department of Biological Sciences, Birkbeck College, London, WC1E 7HX, United Kingdom, Department of Structural and Molecular Biology, University College London, London, WC1E 6BT, United Kingdom; Xu, J.-Y., Department of Structural and Molecular Biology, University College London, London, WC1E 6BT, United Kingdom, Department of Laboratory Medicine and Pathology, University of Alberta, Edmonton, AB T6G 2G3, Canada; Genko, N., Department of Structural and Molecular Biology, University College London, London, WC1E 6BT, United Kingdom; Hartley, A.M., Department of Biological Sciences, Birkbeck College, London, WC1E 7HX, United Kingdom; Haraux, F., Université Paris-Saclay, Commissariat à l’énergie atomique et aux énergies alternatives, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif‐sur‐Yvette, 91198, France; Meunier, B., Université Paris-Saclay, Commissariat à l’énergie atomique et aux énergies alternatives, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif‐sur‐Yve...
推荐引用方式 GB/T 7714	Maréchal A.,Xu J.-Y.,Genko N.,et al. A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria[J],2020,117(17).
APA	Maréchal A..,Xu J.-Y..,Genko N..,Hartley A.M..,Haraux F..,...&Rich P.R..(2020).A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria.Proceedings of the National Academy of Sciences of the United States of America,117(17).
MLA	Maréchal A.,et al."A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria".Proceedings of the National Academy of Sciences of the United States of America 117.17(2020).