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Residues surrounding the active centre of carbon monoxide dehydrogenase are key in converting CO2 to CO

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Abstract

The enzyme carbon monoxide dehydrogenase is capable of efficiently converting \(\hbox {CO}_{2}\) to CO and, therefore, can enable an affordable \(\hbox {CO}_{2}\) recycling strategy. The reduction of \(\hbox {CO}_{2}\) 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 \(\hbox {H}_{2}\hbox {O}\) 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.

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  • 24 September 2021

    Supplementary file has been included to the article.

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Acknowledgements

Via our membership of the UK’s HEC Materials Chemistry Consortium, which is funded by EPSRC (EP/L000202, EP/R029431), this work used the ARCHER UK National Supercomputing Service (http://www.archer.ac.uk). All data supporting this study (the XYZ coordinates of all structures and the metadynamics hills output) are provided as Supplementary Information accompanying this paper.

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  1. Faculty of Medicine and Health Sciences, Crewe Campus, University of Buckingham, Crewe, CW1 5DU, UK

    Umberto Terranova

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Terranova, U. Residues surrounding the active centre of carbon monoxide dehydrogenase are key in converting CO2 to CO. J Biol Inorg Chem 26, 617–624 (2021). https://doi.org/10.1007/s00775-021-01878-4

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