Enzyme-Inspired Assembly: Incorporating Multivariate Interactions to Optimize the Host–Guest Configuration for High-Speed Enantioselective Catalysis

To achieve a rapid asymmetry conversion, the substrate objects suffer from accelerated kinetic velocity and random rotation at the cost of selectivity. Inspired by natural enzymes, optimizing the host–guest configuration will realize the high-performance enantioselective conversion of chemical reactions. Herein, multivariate binding interactions were introduced into the 1D channel of a chiral catalyst to simulate the enzymatic action. An imidazolium group was used to electrophilically activate the C═O unit of a ketone substrate, and the counterion binds the hydrogen donor isopropanol. This binding effect around the catalytic center produces strong stereo-induction, resulting in high conversion (99.5% yield) and enantioselectivity (99.5% ee) for the asymmetric hydrogenation of biomass-derived acetophenone. In addition, the turnover frequency of the resulting catalyst (5160 h–1 TOF) is more than 58 times that of a homogeneous Ru-TsDPEN catalyst (88 h–1 TOF) under the same condition, which corresponds to the best performance reported till date among all existing catalysts for the considered reaction.