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-Structure paper
タイトル | Structural basis for energy transduction by respiratory alternative complex III. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 1728, Year 2018 |
掲載日 | 2018年4月30日 |
著者 | Joana S Sousa / Filipa Calisto / Julian D Langer / Deryck J Mills / Patrícia N Refojo / Miguel Teixeira / Werner Kühlbrandt / Janet Vonck / Manuela M Pereira / |
PubMed 要旨 | Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may ...Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump. |
リンク | Nat Commun / PubMed:29712914 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.87 Å |
構造データ | |
化合物 | ChemComp-HEC: ChemComp-F3S: ChemComp-SF4: |
由来 |
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キーワード | MEMBRANE PROTEIN / electron transfer / quinol oxidation / respiratory chain |