Download MendeleyLight-Activated Artificial CO 2 -Reductase: Structure and Activity.
Labidi, R.J., Faivre, B., Carpentier, P., Perard, J., Gotico, P., Li, Y., Atta, M., Fontecave, M.(2024) J Am Chem Soc
- PubMed: 39352411
- DOI: https://doi.org/10.1021/jacs.4c08927
- Primary Citation of Related Structures:
9F5U, 9F66, 9FVS, 9FW4, 9FY4 - PubMed Abstract:
Light-dependent reduction of carbon dioxide (CO 2 ) into value-added products can be catalyzed by a variety of molecular complexes. Here we report a rare example of a structurally characterized artificial enzyme, resulting from the combination of a heme binding protein, heme oxygenase, with cobalt-protoporphyrin IX, with good activity for the photoreduction of CO 2 to carbon monoxide (CO). Using a copper-based photosensitizer, thus making the photosystem free of noble metals, a large turnover frequency value of ¡«616 h -1 , a turnover value of ¡«589, after 3 h reaction, and a CO vs H 2 selectivity of 72% were obtained, establishing a record among previously reported artificial CO 2 reductases. Thorough photophysical studies allowed tracking of reaction intermediates and provided insights into the reaction mechanism. Thanks to a high-resolution crystal structure of the artificial enzyme, both in the absence and in the presence of the protein-bound CO 2 substrate, a rational site-directed mutagenesis approach was used to study the effect of some modifications of the active site on the activity.
Organizational Affiliation:
Laboratoire de Chimie des Processus Biologiques, UMR 8229, Coll¨¨ge de France, CNRS, Sorbonne Universit¨¦, 11, Place Marcellin-Berthelot, Paris 75005, France.
