A Morphing [4Fe-3S-nO]-Cluster within a Carbon Monoxide Dehydrogenase Scaffold

Journal article

Publication Details

Author list: Jeoung J.H., Fesseler J., Domnik L., Klemke F., Sinnreich M., Teutloff C., Dobbek H.

Journal: Angewandte Chemie International Edition

Publication year: 2022

Volume number: 61

Issue number: 18

Publisher: Wiley-VCH Verlag

ISSN: 1433-7851

eISSN: 1521-3773

DOI: 10.1002/anie.202117000

URL: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85125569783&origin=inward

Languages: English-Great Britain


Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of CO2 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-VCh. Its structure reveals the typical CODH scaffold, but contains an iron-sulfur-oxo hybrid-cluster. Although closely related to true CODHs, CooS-VCh catalyzes neither CO oxidation, nor CO2 reduction. The active site of CooS-VCh undergoes a redox-dependent restructuring between a reduced [4Fe-3S]-cluster and an oxidized [4Fe-2S-S*-2O-2(H2O)]-cluster. Hydroxylamine, a slow-turnover substrate of CooS-VCh, 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.


Last updated on 2022-28-09 at 19:43