Terranova, Umberto (2021) Residues surrounding the active centre of carbon monoxide dehydrogenase are key in converting CO2 to CO. JBIC Journal of Biological Inorganic Chemistry, 26. pp. 617-624. ISSN 1432-1327
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Text (Author's final peer reviewed manuscript)
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Abstract
The enzyme carbon monoxide dehydrogenase is capable of efficiently converting CO2 to CO and therefore can enable an affordable CO2 recycling strategy. The reduction of CO2 occurs at a peculiar nickel-iron-sulfur cluster, following a mechanism that remains little understood. In this study, we have used ab initio molecular dynamics simulations to explore the free energy landscape of the reaction. We predict the existence of a COOH ligand that strongly interacts with the surrounding protein residues and favours a mechanism where a H2O molecule is eliminated before CO. We have taken advantages of the insights offered by our simulations to revisit the catalytic mechanism and the role of the residues surrounding the active centre in particular, thus assisting in the design of inorganic catalysts that mimic the enzyme.
| Item Type: | Article |
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| Additional Information: | Manuscript accepted 17th June 2021. |
| Subjects: | Q Science > QD Chemistry |
| Depositing User: | Umberto Terranova |
| Date Deposited: | 16 Dec 2021 14:24 |
| Last Modified: | 13 Jul 2022 00:15 |
| URI: | http://bear.buckingham.ac.uk/id/eprint/533 |
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