Work

Transferring enzyme features to molecular CO2 reduction catalysts

Year: 2024

Type: review

Abstract: Carbon monoxide dehydrogenases and formate dehydrogenases efficiently catalyze the reduction of CO 2 . In both enzymes, CO 2 activation at the metal active site is assisted by proximate amino acids and Fe–S-clusters. Functional features of the enzyme are mimicked in molecular catalysts by redox-active ligands, acidic and charged groups in the ligand periphery, and binuclear scaffolds. These components have all improved the catalytic performance of synthetic systems. Recent studies impart a deeper understanding of the individual contributions of the various functionalities to reactivity and of their combined effects. New catalyst platforms reveal alternate pathways for CO 2 reduction, unique intermediates, and strategies for switching selectivity. Design of a wider array of complexes that combine different functional elements is encouraged to further optimize catalysts for CO 2 reduction, especially for product formation beyond CO. More diverse bimetallic catalysts are needed to better exploit metal–metal interactions for CO 2 conversion.

Source: Current Opinion in Chemical Biology

DOI: 10.1016/j.cbpa.2024.102540

Authors: Matthias Huber, Corinna R. Hess

Institution: University of Regensburg

Language: English

Topic: CO2 Reduction Techniques and Catalysts

Subfield: Renewable Energy, Sustainability and the Environment

Field: Energy

Domain: Physical Sciences

SDG: Climate action

Open Access status: hybrid

Estimated APC paid: $4,660