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April 3, 2026Chemical Science1 citationsOpen Access

A protein-based model of carbon monoxide dehydrogenase exhibits tunable covalency across cluster oxidation and ligand-bound states

LLLuke C. LewisPBPrajakta BadveIVItzel P Vaca

Key Points

  • The aim is to explore the tunable covalency of the C-cluster in carbon monoxide dehydrogenase.
  • Modeling of the protein-based carbon monoxide dehydrogenase
  • Comparison of covalency across different oxidation states
  • Analysis of ligand-bound effects on catalytic activity
  • Covalency varies significantly between different oxidation states of the C-cluster
  • Ligand-binding influences the efficiency of CO2 reduction
  • The model accurately replicates the behavior of natural CODH under various conditions

Abstract

The nickel-containing carbon monoxide dehydrogenase (CODH) uses a unique heterometallic NiFe 4 S 4 cluster active site, called the C-cluster, to catalyze the reversible reduction of carbon dioxide (CO 2 ) to carbon monoxide (CO)...

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Cite This Study

Lewis et al. (2026) studied this question.

synapsesocial.com/papers/69cf5ebc5a333a821460d48ehttps://doi.org/10.1039/d6sc00023a
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