JOM KITA KE POLITEKNIK

Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates? (Record no. 2240)

MARC details
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Personal name Chung, Injae
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9 (RLIN) 3148
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Title Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?
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Date of publication, distribution, etc. 2022-12-01.
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General note /pmc/articles/PMC7614202/
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General note /pubmed/36087446
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Summary, etc. Respiratory complex I (NADH:ubiquinone oxidoreductase) is a multi-subunit, energy-transducing mitochondrial enzyme that is essential for oxidative phosphorylation and regulating NAD(+)/NADH pools. Despite recent advances in structural knowledge and a long history of biochemical analyses, the mechanism of redox-coupled proton translocation by complex I remains unknown. Due to its ability to separate molecules in a mixed population into distinct classes, single-particle electron cryomicroscopy has enabled identification and characterisation of different complex I conformations. However, deciding on their catalytic and/or regulatory properties to underpin mechanistic hypotheses, especially without detailed biochemical characterisation of the structural samples, has proven challenging. In this review we explore different mechanistic interpretations of the closed and open states identified in cryoEM analyses of mammalian complex I.
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Terms governing use and reproduction
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Terms governing use and reproduction https://creativecommons.org/licenses/by/4.0/This work is licensed under a CC BY 4.0 (https://creativecommons.org/licenses/by/4.0/) International license.
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Language note en
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Topical term or geographic name as entry element Article
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Genre/form data or focus term Text
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Personal name Grba, Daniel N.
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9 (RLIN) 3149
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Personal name Wright, John J.
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9 (RLIN) 3150
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Personal name Hirst, Judy
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9 (RLIN) 3151
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Note Curr Opin Struct Biol
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Uniform Resource Identifier <a href="http://dx.doi.org/10.1016/j.sbi.2022.102447">http://dx.doi.org/10.1016/j.sbi.2022.102447</a>
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