Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 27, Issue 10, Pages 892-+Publisher
NATURE RESEARCH
DOI: 10.1038/s41594-020-0473-x
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Funding
- Wellcome Trust
- MRC
- BBSRC
- Medical Research Council [MC_U105663141, MC_UU_00015/2]
- MRC [MC_UU_00015/2] Funding Source: UKRI
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Mitochondrial complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from ubiquinone reduction by NADH to drive protons across the energy-transducing inner membrane. Recent cryo-EM analyses of mammalian and yeast complex I have revolutionized structural and mechanistic knowledge and defined structures in different functional states. Here, we describe a 2.7-angstrom-resolution structure of the 42-subunit complex I from the yeastYarrowia lipolyticacontaining 275 structured water molecules. We identify a proton-relay pathway for ubiquinone reduction and water molecules that connect mechanistically crucial elements and constitute proton-translocation pathways through the membrane. By comparison with known structures, we deconvolute structural changes governing the mammalian 'deactive transition' (relevant to ischemia-reperfusion injury) and their effects on the ubiquinone-binding site and a connected cavity in ND1. Our structure thus provides important insights into catalysis by this enigmatic respiratory machine. A cryo-EM structure of mitochondrial complex I fromYarrowia lipolyticareveals structured waters involved in proton relays and energy transfer, with insights into the 'deactive transition' in mammalian systems.
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