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			_c1010 _d1010