A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase
説明
Bovine cytochrome c oxidase (CcO), a 420-kDa membrane protein, pumps protons using electrostatic repulsion between protons transferred through a water channel and net positive charges created by oxidation of heme a (Fe-a) for reduction of O-2 at heme a(3) (Fe-a3). For this process to function properly, timing is essential: The channel must be closed after collection of the protons to be pumped and before Fea oxidation. If the channel were to remain open, spontaneous backflow of the collected protons would occur. For elucidation of the channel closure mechanism, the opening of the channel, which occurs upon release of CO from CcO, is investigated by newly developed time-resolved x-ray free-electron laser and infrared techniques with nanosecond time resolution. The opening process indicates that Cu-B senses completion of proton collection and binds O-2 before binding to Fe-a3 to close the water channel using a conformational relay system, which includes Cu-B, heme a(3), and a transmembrane helix, to block backflow of the collected protons.
収録刊行物
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- Science Advances
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Science Advances 3 (7), e1603042-e1603042, 2017-07
American Association for the Advancement of Science
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詳細情報 詳細情報について
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- CRID
- 1050575520346942592
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- NII論文ID
- 120006363290
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- ISSN
- 23752548
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- HANDLE
- 20.500.14094/90004338
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- PubMed
- 28740863
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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