Formate dehydrogenases for CO2 utilization

Abstract

New measures for reducing atmospheric CO₂ are urgently needed. Formate dehydrogenases (FDHs, EC 1.17.1.9) catalyze conversion of CO₂ to formate (HCOO^-) via a reverse catalytic ability. This enzymatic conversion of CO₂ represents a novel first step approach for biocatalytic carbon capture and utilization targeting both CO₂ reduction and substitution of petrochemical-based production of important commodity chemicals. To achieve robust and efficient FDH catalyzed CO₂ conversion for sustainable large-scale implementation, it is critical to focus on the efficacy of the electron donor, enzyme stabilization, and on how the desired reverse FDH reactivity can be enhanced. Recent advances include the realization that NADH, the most common natural cofactor for reverse FDH catalysis, is an inefficient electron donor for FDH catalyzed CO₂ conversion. Improved understanding of the redox reaction details and structure-function relations of both metal-dependent and metal-independent FDHs provides the foundation for achieving rational technological advancements to promote enzymatic CO₂ utilization.