Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 77, Issue -, Pages -Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2022.102447
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Funding
- Medical Research Council
- [MC_UU_00015/2]
- [MC_UU_00028/1]
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In this review, we explore different mechanistic interpretations of the closed and open states identified in cryoEM analyses of mammalian complex I.
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 un-known. Due to its ability to separate molecules in a mixed population into distinct classes, single-particle electron cryo-microscopy 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 charac-terisation 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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