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Updated: Aug 7, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Orthogonal Expression of an Artificial Metalloenzyme for Abiotic Catalysis
Evan W Reynolds1, Timothy D Schwochert1, Matthew W McHenry1
1Department of Chemistry, University of North Carolina at Chapel Hill, 125 South Road CB 3290, Chapel Hill, North Carolina, 27599, USA.
Abstract:
A cytochrome P450 was engineered to selectively incorporate Ir(Me)-deuteroporphyrin IX (Ir(Me)-DPIX), in lieu of heme, in bacterial cells. Cofactor selectivity was altered by introducing mutations within the heme-binding pocket to discriminate the deuteroporphyrin macrocycle, in combination with mutations to the P450 axial cysteine to accommodate a pendant methyl group on the Ir(Me) center. This artificial metalloenzyme was investigated for activity in non-native metallocarbenoid-mediated olefin cyclopropanation reactions and showed enhanced activity for aliphatic and electron-deficient olefins when compared to the native heme enzyme. This work provides a general strategy to augment the chemical functionality of heme enzymes in cells with application towards abiotic catalysis.
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