globalchange  > 气候变化与战略
DOI: 10.1073/pnas.2001572117
论文题名:
A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria
作者: Maréchal A.; Xu J.-Y.; Genko N.; Hartley A.M.; Haraux F.; Meunier B.; Rich P.R.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期:17
起始页码: 9349
结束页码: 9355
语种: 英语
英文关键词: ADP/O ratio ; Cytochrome c oxidase ; H/e stoichiometry ; Mitochondria ; Proton pumping
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
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.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163473
Appears in Collections:气候变化与战略

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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‐Yvette, 91198, France; Rich, P.R., Department of Structural and Molecular Biology, University College London, London, WC1E 6BT, United Kingdom

Recommended Citation:
Maréchal A.,Xu J.-Y.,Genko N.,et al. A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(17)
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