Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation

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Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO2 to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the Desulfovibrio vulgaris Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of DvFdhAB in crystals was confirmed by reduction and reoxidation structural studies.

Original languageEnglish
Article number476
Number of pages9
JournalInternational Journal of Molecular Sciences
Issue number1
Publication statusPublished - 28 Dec 2022


  • CO reduction
  • formate dehydrogenase
  • molybdopterin
  • redox enzymes
  • tungsten cofactor
  • X-ray crystallography


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