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Experimental study demonstrates stereoselective epoxidation by copper-albumin artificial enzymes, highlighting the utility of noncatalytic proteins for chiral synthesis.
We herein report a design of artificial enzymes by incorporating a synthetic copper complex into noncatalytic bovine serum albumin (Cu-BSA) to carry out stereoselective oxidation. This Cu-BSA catalyst with stably bound Cu complex as a cofactor shows peroxidase-like activity to catalyze epoxidation of styrene with high chiral selectivity (>99%) to R-styrene epoxide. With the electrochemical conversion of Cu 2+ to Cu +, Cu-BSA also exhibits oxidase-like activity to selectively reduce oxygen to hydrogen peroxide (H 2 O 2 ), which can be combined with its peroxidase function to drive oxidation of C═C bonds using air. This artificial enzymatic system holds promise for chiral-selective transformations of non-natural substances and highlights the versatility of noncatalytic proteins in the design of artificial enzymes.
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Liaqat et al. (2024) studied this question.
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