000 01866 am a22002413u 4500
042 _adc
100 1 0 _aChung, Injae
_eauthor
_93148
700 1 0 _aGrba, Daniel N.
_eauthor
_93149
700 1 0 _aWright, John J.
_eauthor
_93150
700 1 0 _aHirst, Judy
_eauthor
_93151
245 0 0 _aMaking the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?
260 _c2022-12-01.
500 _a/pmc/articles/PMC7614202/
500 _a/pubmed/36087446
520 _aRespiratory 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.
540 _a
540 _ahttps://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.
546 _aen
690 _aArticle
655 7 _aText
_2local
786 0 _nCurr Opin Struct Biol
856 4 1 _uhttp://dx.doi.org/10.1016/j.sbi.2022.102447
_zConnect to this object online.
999 _c2240
_d2240