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Title: Exploring the binding pocket of quinone/inhibitors in mitochondrial respiratory complex I by chemical biology approaches
Authors: Murai, Masatoshi  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-6601-2854 (unconfirmed)
Author's alias: 村井, 正俊
Keywords: Respiratory complex I
mitochondria
inhibitor
ubiquinone
chemical biology
Issue Date: 2-Jul-2020
Publisher: Taylor & Francis Group
Journal title: Bioscience, Biotechnology, and Biochemistry
Volume: 84
Start page: 1322
End page: 1331
Abstract: NADH-quinone oxidoreductase (respiratory complex I) is a key player in mitochondrial energy metabolism. The enzyme couples electron transfer from NADH to quinone with the translocation of protons across the membrane, providing a major proton-motive force that drives ATP synthesis. Recently, X-ray crystallography and cryo-electron microscopy provided further insights into the structure and functions of the enzyme. However, little is known about the mechanism of quinone reduction, which is a crucial step in the energy coupling process. A variety of complex I inhibitors targeting the quinone-binding site have been indispensable tools for mechanistic studies on the enzyme. Using biorationally designed inhibitor probes, the author has accumulated a large amount of experimental data characterizing the actions of complex I inhibitors. On the basis of comprehensive interpretations of the data, the author reviews the structural features of the binding pocket of quinone/inhibitors in bovine mitochondrial complex I.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis Group in 'Bioscience, Biotechnology, and Biochemistry' on 2020, available online: https://www.tandfonline.com/10.1080/09168451.2020.1747974
The full-text file will be made open to the public on 07 Apr 2021 in accordance with publisher's 'Terms and Conditions for Self-Archiving'
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
URI: http://hdl.handle.net/2433/253575
DOI(Published Version): 10.1080/09168451.2020.1747974
PubMed ID: 32264779
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