7B97

CooS-V with oxidized hybrid cluster by hydroxylamine for 30 min

7B97 の概要

• エントリーDOI: 10.2210/pdb7b97/pdb
• 分子名称: Carbon monoxide dehydrogenase, FE2/S2 (INORGANIC) CLUSTER, IRON/SULFUR CLUSTER, ... (7 entities in total)
• 機能のキーワード: hybrid cluster, hcp, codh, oxidoreductase
• 由来する生物種: Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 138522.40

構造登録者

Jeoung, J.H.,Dobbek, H. (登録日: 2020-12-14, 公開日: 2022-01-12, 最終更新日: 2024-01-31)

主引用文献

Jeoung, J.H.,Fesseler, J.,Domnik, L.,Klemke, F.,Sinnreich, M.,Teutloff, C.,Dobbek, H.
A Morphing [4Fe-3S-nO]-Cluster within a Carbon Monoxide Dehydrogenase Scaffold.
Angew.Chem.Int.Ed.Engl., 61:e202117000-e202117000, 2022

PubMed Abstract: Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of CO to CO. Several anaerobic microorganisms encode multiple CODHs in their genome, of which some, despite being annotated as CODHs, lack a cysteine of the canonical binding motif for the active site Ni,Fe-cluster. Here, we report on the structure and reactivity of such a deviant enzyme, termed CooS-V . Its structure reveals the typical CODH scaffold, but contains an iron-sulfur-oxo hybrid-cluster. Although closely related to true CODHs, CooS-V catalyzes neither CO oxidation, nor CO reduction. The active site of CooS-V undergoes a redox-dependent restructuring between a reduced [4Fe-3S]-cluster and an oxidized [4Fe-2S-S*-2O-2(H O)]-cluster. Hydroxylamine, a slow-turnover substrate of CooS-V , oxidizes the hybrid-cluster in two structurally distinct steps. Overall, minor changes in CODHs are sufficient to accommodate a Fe/S/O-cluster in place of the Ni,Fe-heterocubane-cluster of CODHs.

PubMed: 35133707
DOI: 10.1002/anie.202117000

実験手法

X-RAY DIFFRACTION (1.45 Å)