7B9A

CooS-V with Xe-soaked

Summary for 7B9A

• Entry DOI: 10.2210/pdb7b9a/pdb
• Descriptor: Carbon monoxide dehydrogenase, IRON/SULFUR CLUSTER, XENON, ... (7 entities in total)
• Functional Keywords: hybrid cluster, hcp, codh, oxidoreductase
• Biological source: Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
• Total number of polymer chains: 4
• Total formula weight: 286136.42

Authors

Jeoung, J.H.,Dobbek, H. (deposition date: 2020-12-14, release date: 2022-01-12, Last modification date: 2024-01-31)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)