| Autor: |
Grba DN; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK., Hirst J; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK. jh@mrc-mbu.cam.ac.uk. |
| Jazyk: |
angličtina |
| Zdroj: |
Nature structural & molecular biology [Nat Struct Mol Biol] 2020 Oct; Vol. 27 (10), pp. 892-900. Date of Electronic Publication: 2020 Aug 03. |
| DOI: |
10.1038/s41594-020-0473-x |
| Abstrakt: |
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-Å-resolution structure of the 42-subunit complex I from the yeast Yarrowia lipolytica containing 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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