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9TP0

CO dehydrogenase 2 variant A559W V610H

9TP0 の概要
エントリーDOI10.2210/pdb9tp0/pdb
分子名称Carbon monoxide dehydrogenase 2, IRON/SULFUR CLUSTER, FE2/S2 (INORGANIC) CLUSTER, ... (6 entities in total)
機能のキーワードcodh, channel, a559w, cluster c, 4fe-4s, iron, iron-sulfur, nickel, oxidoreductase
由来する生物種Carboxydothermus hydrogenoformans Z-2901
タンパク質・核酸の鎖数1
化学式量合計67981.24
構造登録者
Gebhardt, P.,Dobbek, H.,Jeoung, J.-H. (登録日: 2025-12-17, 公開日: 2026-06-03)
主引用文献Opdam, L.V.,Gebhardt, P.,Leger, C.,Dobbek, H.,Fourmond, V.
Correspondence on "Fortification of FeS Clusters Reshapes Anaerobic CO Dehydrogenase Into an Air-Viable Enzyme Through Multilayered Sealing of O 2 Tunnels".
Angew.Chem.Int.Ed.Engl., :e1942100-e1942100, 2026
Cited by
PubMed Abstract: In their recent communication in Angewandte Chemie (10.1002/anie.202508565), Suk Min Kim and coworkers have described the effect of modifying the gas channels of the CO dehydrogenase II from Carboxydothermus hydrogenoformans, an enzyme that oxidizes reversibly CO into CO. Their goal was to use mutagenesis to slow down the arrival of O at the active site. They reported a large increase in the resistance against oxygen, one of the major barriers to the application of this extremely fast and efficient enzyme in biotechnological devices, with an increase in the IC of more than two orders of magnitudes for some variants, with only a minor impact on the affinity of the enzyme for CO. We have produced the same variants, and characterized them in depth using Protein Film Electrochemistry. We used an approach that has proven very useful to learn and understand about the reactivity of CO dehydrogenases (and other redox enzymes like hydrogenases) with O. We found that, contrary to the claims by Kim and coworkers, the A559W and the A559W/V610H mutants are not more resistant than the wild type against oxygen.
PubMed: 42175862
DOI: 10.1002/anie.1942100
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.41 Å)
構造検証レポート
Validation report summary of 9tp0
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-07-08に公開中

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