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-Structure paper
| タイトル | Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria. |
|---|---|
| ジャーナル・号・ページ | Nat Chem Biol, Vol. 21, Issue 7, Page 1058-1068, Year 2025 |
| 掲載日 | 2025年1月29日 |
著者 | Ashleigh Kropp / David L Gillett / Hari Venugopal / Miguel A Gonzálvez / James P Lingford / Surbhi Jain / Christopher K Barlow / Jie Zhang / Chris Greening / Rhys Grinter / ![]() |
| PubMed 要旨 | Diverse bacteria and archaea use atmospheric CO as an energy source for long-term survival. Bacteria use [MoCu]-CO dehydrogenases (Mo-CODH) to convert atmospheric CO to carbon dioxide, transferring ...Diverse bacteria and archaea use atmospheric CO as an energy source for long-term survival. Bacteria use [MoCu]-CO dehydrogenases (Mo-CODH) to convert atmospheric CO to carbon dioxide, transferring the obtained electrons to the aerobic respiratory chain. However, it is unknown how these enzymes oxidize CO at low concentrations and interact with the respiratory chain. Here, we use cryo-electron microscopy and structural modeling to show how Mo-CODH (CoxSML) from Mycobacterium smegmatis interacts with its partner, the membrane-bound menaquinone-binding protein CoxG. We provide electrochemical, biochemical and genetic evidence that Mo-CODH transfers CO-derived electrons to the aerobic respiratory chain through CoxG. Lastly, we show that Mo-CODH and CoxG genetically and structurally associate in diverse bacteria and archaea. These findings reveal the basis of the biogeochemically and ecologically important process of atmospheric CO oxidation, while demonstrating that long-range quinone transport is a general mechanism of energy conservation, which convergently evolved on multiple occasions. |
リンク | Nat Chem Biol / PubMed:39881213 / PubMed Central |
| 手法 | EM (単粒子) / X線回折 |
| 解像度 | 1.5 - 1.85 Å |
| 構造データ | EMDB-42164, PDB-8uem: ![]() PDB-8uds: |
| 化合物 | ![]() ChemComp-HOH: ![]() ChemComp-CUN: ![]() ChemComp-MCN: ![]() ChemComp-FAD: ![]() ChemComp-FES: |
| 由来 |
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キーワード | ELECTRON TRANSPORT / Menaquinone Binding / Lipid Anchored / Carbon monoxide dehydrogenase / SRPBCC family protein / OXIDOREDUCTASE / MoCu / Mycobacterium smegmatis / High affinity / trace gas scavenging |
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mycolicibacterium smegmatis mc2 155 (バクテリア)
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