Nature structural & molecular biology, 2020-10, Vol.27 (10), p.892
2020
Details
- Autor(en) / Beteiligte
- Titel
- Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation
- Ist Teil von
- Nature structural & molecular biology, 2020-10, Vol.27 (10), p.892
- Ort / Verlag
- United States
- Erscheinungsjahr
- 2020
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- eISSN: 1545-9985DOI: 10.1038/s41594-020-0473-xTitel-ID: cdi_pubmed_primary_32747785
- Format
- –
- Schlagworte
- Binding Sites, Catalysis, Crystallography, X-Ray, Electron Transport Complex I - chemistry, Electron Transport Complex I - metabolism, Models, Molecular, Protein Conformation, Protein Domains, Protein Subunits, Protons, Ubiquinone - analogs & derivatives, Ubiquinone - chemistry, Ubiquinone - metabolism, Water - metabolism, Yarrowia - chemistry