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-Structure paper
タイトル | Key role of quinone in the mechanism of respiratory complex I. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 4135, Year 2020 |
掲載日 | 2020年8月18日 |
著者 | Javier Gutiérrez-Fernández / Karol Kaszuba / Gurdeep S Minhas / Rozbeh Baradaran / Margherita Tambalo / David T Gallagher / Leonid A Sazanov / |
PubMed 要旨 | Complex I is the first and the largest enzyme of respiratory chains in bacteria and mitochondria. The mechanism which couples spatially separated transfer of electrons to proton translocation in ...Complex I is the first and the largest enzyme of respiratory chains in bacteria and mitochondria. The mechanism which couples spatially separated transfer of electrons to proton translocation in complex I is not known. Here we report five crystal structures of T. thermophilus enzyme in complex with NADH or quinone-like compounds. We also determined cryo-EM structures of major and minor native states of the complex, differing in the position of the peripheral arm. Crystal structures show that binding of quinone-like compounds (but not of NADH) leads to a related global conformational change, accompanied by local re-arrangements propagating from the quinone site to the nearest proton channel. Normal mode and molecular dynamics analyses indicate that these are likely to represent the first steps in the proton translocation mechanism. Our results suggest that quinone binding and chemistry play a key role in the coupling mechanism of complex I. |
リンク | Nat Commun / PubMed:32811817 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 3.109 - 6.1 Å |
構造データ | EMDB-11231, PDB-6ziy: EMDB-11235, PDB-6zjl: EMDB-11237, PDB-6zjn: EMDB-11238, PDB-6zjy: PDB-6i0d: PDB-6i1p: PDB-6q8o: PDB-6q8w: PDB-6q8x: PDB-6y11: |
化合物 | ChemComp-SF4: ChemComp-FMN: ChemComp-FES: ChemComp-DCQ: ChemComp-NAI: ChemComp-HQH: ChemComp-HQW: ChemComp-HQK: |
由来 |
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キーワード | MEMBRANE PROTEIN / Respiratory chain / complex I / NADH:ubiquinone oxidoreductase / electron transfer / proton translocation |