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-Structure paper
タイトル | Cryo-EM structure of respiratory complex I at work. |
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ジャーナル・号・ページ | Elife, Vol. 7, Year 2018 |
掲載日 | 2018年10月2日 |
著者 | Kristian Parey / Ulrich Brandt / Hao Xie / Deryck J Mills / Karin Siegmund / Janet Vonck / Werner Kühlbrandt / Volker Zickermann / |
PubMed 要旨 | 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. |
リンク | Elife / PubMed:30277212 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.32 - 4.51 Å |
構造データ | EMDB-4384, PDB-6gcs: EMDB-4385: |
化合物 | ChemComp-SF4: ChemComp-FES: ChemComp-FMN: ChemComp-NDP: ChemComp-ZN: ChemComp-ZMP: ChemComp-CDL: ChemComp-3PE: |
由来 |
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キーワード | OXIDOREDUCTASE / Complex I / NADH dehydrogenase / Mitochondrion Proton pumping / Ubiquinone |