期刊
STRUCTURE
卷 26, 期 2, 页码 312-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.12.014
关键词
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资金
- Wellcome Trust [EM13581]
- MRC [EM13581]
- BBSRC [EM13581]
- Medical Research Council [U105663141, U105184322]
- Medical Research Council [MC_UU_00015/2, MC_U105184322, MC_U105663141] Funding Source: researchfish
- MRC [MC_UU_00015/2, MC_U105663141, MC_U105184322] Funding Source: UKRI
Complex I (NADH: ubiquinone oxidoreductase) is central to energy metabolism in mammalian mitochondria. It couples NADH oxidation by ubiquinone to proton transport across the energy-conserving inner membrane, catalyzing respiration and driving ATP synthesis. In the absence of substrates, active complex I gradually enters a pronounced resting or deactive state. The active-deactive transition occurs during ischemia and is crucial for controlling how respiration recovers upon reperfusion. Here, we set a highly active preparation of Bos taurus complex I into the biochemically defined deactive state, and used single-particle electron cryomicroscopy to determine its structure to 4.1 angstrom resolution. We show that the deactive state arises when critical structural elements that form the ubiquinone-binding site become disordered, and we propose reactivation is induced when substrate binding to the NADH-reduced enzyme templates their reordering. Our structure both rationalizes biochemical data on the deactive state and offers new insights into its physiological and cellular roles.
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