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Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation by Daniel N. Grba; Judy Hirst is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation about?
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.
Who reads Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Daniel N. Grba; Judy Hirst
- Publisher
- Springer Science and Business Media LLC
- Published
- 2020
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)