9FVS

Crystal structure of Heme-Oxygenase mutant G139A from Corynebacterium diphtheriae complexed with Cobalt-porphyrine (HumO-Co(III))

Summary for 9FVS

• Entry DOI: 10.2210/pdb9fvs/pdb
• Related: 9F5U 9F66
• Descriptor: heme oxygenase (biliverdin-producing), PROTOPORPHYRIN IX CONTAINING CO, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: carbon dioxide photoreduction artificial enzyme cobalt-porphyrin heme-oxygenase oxidoreductase, oxidoreductase
• Biological source: Corynebacterium diphtheriae
• Total number of polymer chains: 1
• Total formula weight: 24839.21

Authors

Labidi, R.J.,Faivre, B.,Carpentier, P.,Perard, J.,Gotico, P.,Li, Y.,Atta, M.,Fontecave, M. (deposition date: 2024-06-28, release date: 2024-10-16)

Primary citation

Labidi, R.J.,Faivre, B.,Carpentier, P.,Perard, J.,Gotico, P.,Li, Y.,Atta, M.,Fontecave, M.
Light-Activated Artificial CO 2 -Reductase: Structure and Activity.
J.Am.Chem.Soc., 2024

PubMed Abstract: Light-dependent reduction of carbon dioxide (CO) 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 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, a turnover value of ∼589, after 3 h reaction, and a CO vs H selectivity of 72% were obtained, establishing a record among previously reported artificial CO 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 substrate, a rational site-directed mutagenesis approach was used to study the effect of some modifications of the active site on the activity.

PubMed: 39352411
DOI: 10.1021/jacs.4c08927

Experimental method

X-RAY DIFFRACTION (1.4 Å)