期刊
SCIENCE
卷 316, 期 5821, 页码 85-88出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1138748
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Although many enzymes can promote chemical reactions by tuning substrate properties purely through the electrostatic environment of a docking cavity, this strategy has proven challenging to mimic in synthetic host-guest systems. Here, we report a highly charged, water-soluble, metal-ligand assembly with a hydrophobic interior cavity that thermodynamically stabilizes protonated substrates and consequently catalyzes the normally acidic hydrolysis of orthoformates in basic solution, with rate accelerations of up to 890-fold. The catalysis reaction obeys Michaelis-Menten kinetics and exhibits competitive inhibition, and the substrate scope displays size selectivity, consistent with the constrained binding environment of the molecular host.
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