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Abstract: Zinc enzymes are ubiquitous in nature and are frequently used to catalyze the hydrolysis of carboxylic acid esters, phosphate esters, and amides. Although many models and mimics of zinc enzymes have been reported, it remains difficult to construct active sites with accurately positioned catalytic groups and tunable substrate selectivity. By imprinting a substrate-like amino template coordinated to a polymerizable zinc complex inside cross-linked micelles, we prepared water-soluble nanoparticles with well-defined active sites. The position of the zinc ion could be tuned systematically with respect to the ester bond to be cleaved in the substrate (p-nitrophenyl esters), as well as the rigidity of the active site. Our imprinted zinc catalysts were able to distinguish substrates that differed by the position of a single methyl group, chain length of the acyl chain, and substitution of the phenyl ring. The turnover number (>460 at pH 7) was 1 order of magnitude higher than those previously reported for artificial zinc enzymes in the literature
Template and target information: catalyst, transition state analogue, TSA
Author keywords: active site, artificial enzyme, biomimetic catalysis, hydrolysis, Michaelis-Menten, molecular imprinting, selectivity