+Search query
-Structure paper
Title | Cryo-EM structure of respiratory complex I at work. |
---|---|
Journal, issue, pages | Elife, Vol. 7, Year 2018 |
Publish date | Oct 2, 2018 |
Authors | Kristian Parey / Ulrich Brandt / Hao Xie / Deryck J Mills / Karin Siegmund / Janet Vonck / Werner Kühlbrandt / Volker Zickermann / |
PubMed Abstract | Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 ...Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 MDa membrane protein complex transfers electrons from NADH to ubiquinone, providing the energy to drive proton pumping at distant sites in the membrane arm. The critical steps of energy conversion are associated with the redox chemistry of ubiquinone. We report the cryo-EM structure of complete mitochondrial complex I from the aerobic yeast both in the deactive form and after capturing the enzyme during steady-state activity. The site of ubiquinone binding observed during turnover supports a two-state stabilization change mechanism for complex I. |
External links | Elife / PubMed:30277212 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.32 - 4.51 Å |
Structure data | EMDB-4384, PDB-6gcs: EMDB-4385: |
Chemicals | ChemComp-SF4: ChemComp-FES: ChemComp-FMN: ChemComp-NDP: ChemComp-ZN: ChemComp-ZMP: ChemComp-CDL: ChemComp-3PE: |
Source |
|
Keywords | OXIDOREDUCTASE / Complex I / NADH dehydrogenase / Mitochondrion Proton pumping / Ubiquinone |