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Abstract
Natural enzymes exhibit unparalleled selectivity due to the microenvironment around the active sites, but how to design artificial catalysts to achieve similar performance is a formidable challenge for the catalysis community. Herein, we report that a less selective platinum catalyst becomes highly active and selective for industrially relevant hydrosilylation of a broad range of substrates when a porous cage ligand is used for confinement around the catalytic active site. The catalyst is more than ten times more active than Karstedt’s catalyst while being recyclable. Properties such as size-selective catalysis and Michaelis-Menten kinetics support the proposed enzyme-like model. This biomimetic catalyst exhibits remarkable site-selectivity through the cage’s confining effect, which amplifies small steric differences into dramatic reactivity changes for similar functional groups within a molecule.
Design of artificial catalysts to mimic enzyme activity and selectivity is a challenge in the catalysis field. Here, the authors design a platinum catalyst with a porous cage ligand which shows enzyme-like properties, such as high hydrosilylation activity and substrate size selectivity, while being recyclable.
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1 Beihang University, School of Chemistry, Beijing, PR China (GRID:grid.64939.31) (ISNI:0000 0000 9999 1211)
2 New York University, The Department of Chemistry, New York, USA (GRID:grid.137628.9) (ISNI:0000 0004 1936 8753)
3 Beijing University of Chemical Technology, Chaoyang, Center for Instrumental Analysis, Beijing, PR China (GRID:grid.48166.3d) (ISNI:0000 0000 9931 8406)
4 Chinese Academy of Sciences, Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Beijing, PR China (GRID:grid.9227.e) (ISNI:0000000119573309)
5 Beihang University, School of Chemistry, Beijing, PR China (GRID:grid.64939.31) (ISNI:0000 0000 9999 1211); Beihang University, Beijing Advanced Innovation Center for Biomedical Engineering, Beijing, PR China (GRID:grid.64939.31) (ISNI:0000 0000 9999 1211)