Formate dehydrogenases for CO2 utilization

• Published in: Current opinion in biotechnology Vol. 73; pp. 95 - 100
• Main Authors: Calzadiaz-Ramirez, Liliana, Meyer, Anne S
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.02.2022
• ISSN: 0958-1669; 1879-0429
• DOI: 10.1016/j.copbio.2021.07.011

[Display omitted] •Formate dehydrogenases (FDHs) can catalyze reduction of CO2 to HCOO−.•Immobilization can improve FDH kinetics for CO2 reduction.•Non-natural electron donors are better than NADH for FDH catalyzed CO2 conversion.•Multi-enzyme cascades with FDH have potential for methanol production.•Formatotrophic microorganisms can utilize CO2 via FDH. 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.