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Carbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase
Abstract
Anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO 2 at a complex Ni-, Fe-, and S-containing metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO 2 supplied in solution is bound and reductively activated by cluster C. In the intermediate structure, CO 2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO 2 reduction at the Ni-Fe site of cluster C.
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Great Metalloclusters in Enzymology
Rees, D. C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135406 · Cited by 220
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Dalle, K. E., Warnan, J., Leung, J. J., Reuillard, B., Karmel, I. S., & Reisner, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00392 · Cited by 912
Liu, L., & Corma, A. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00733 · Cited by 689
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Metadata
- Authors
- Jeoung, J.-H., & Dobbek, H.
- Venue
- Science
- Published
- 2007-11-30
- Volume
- 318
- Issue
- 5855
- Pages
- 1461-1464
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2009436238
- Cited by
- 625
- References
- 1
- FWCI
- 9.49
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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