9fw4
Crystal structure of Heme-Oxygenase mutant H20C from Corynebacterium diphtheriae complexed with Cobalt-porphyrine (HumO-Co(III))Crystal structure of Heme-Oxygenase mutant H20C from Corynebacterium diphtheriae complexed with Cobalt-porphyrine (HumO-Co(III))
Structural highlights
FunctionPublication Abstract from PubMedLight-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 approximately 616 h(-1), a turnover value of approximately 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. Light-Activated Artificial CO(2)-Reductase: Structure and Activity.,Labidi RJ, Faivre B, Carpentier P, Perard J, Gotico P, Li Y, Atta M, Fontecave M J Am Chem Soc. 2024 Oct 1. doi: 10.1021/jacs.4c08927. PMID:39352411[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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