Chaetomium thermophilum formate dehydrogenase has high activity in the reduction of hydrogen carbonate (HCO3-) to formate

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Aslan A. S. , Valjakka J., Ruupunen J., YILDIRIM D., Turner N. J. , Turunen O., ...More

PROTEIN ENGINEERING DESIGN & SELECTION, vol.30, no.1, pp.47-55, 2017 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 30 Issue: 1
  • Publication Date: 2017
  • Doi Number: 10.1093/protein/gzw062
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.47-55
  • Keywords: biotransformation of CO2, catalytic mechanism, kinetic parameters with hydrogen carbonate, molecular modeling, NAD(+)-dependent formate dehydrogenase, NAD(+)-DEPENDENT FORMATE, CATALYTIC MECHANISM, FORMIC-ACID, CONVERSION, DIOXIDE, CO2, BIOCATALYSTS


While formate dehydrogenases (FDHs) have been used for cofactor recycling in chemoenzymatic synthesis, the ability of FDH to reduce CO2 could also be utilized in the conversion of CO2 to useful products via formate (HCOO-). In this study, we investigated the reduction of CO2 in the form of hydrogen carbonate (HCO3-) to formate by FDHs from Candida methylica (CmFDH) and Chaetomium thermophilum (CtFDH) in a NADH-dependent reaction. The catalytic performance with HCO(3)w(-) as a substrate was evaluated by measuring the kinetic rates and conducting productivity assays. CtFDH showed a higher efficiency in converting HCO3- to formate than CmFDH, whereas CmFDH was better in the oxidation of formate. The pH optimum of the reduction was at pH 7-8. However, the high concentrations of HCO3- reduced the reaction rate. CtFDH was modeled in the presence of HCO3- showing that it fits to the active site. The active site setting for hydride transfer in CO2 reduction was modeled. The hydride donated by NADH would form a favorable contact to the carbon atom of HCO3-, resulting in a surplus of electrons within the molecule. This would cause the complex formed by hydrogen carbonate and the hydride to break into formate and hydroxide ions.