Selective Catalytic Oxidation of Substrates That Bind to Metalloporphyrin Enzyme Mimics Carrying Two or Four Cyclodextrin Groups and Related Metallosaiens

摘要

Although the speed of enzyme-eatalyzed reactions is to be admired and imitated, the most useful enzyme catalytic property is its selectivity. Our invention of remote oxidation was inspired by the ability of enzymes to hold their substrates in such a geometry that reaction is directed to specific substrate atoms. However, the use of a covalent link between substrate and catalyst prevented catalytic turnover. To avoid this problem, we created a metalloporphyrin catalyst carrying two additional metal ions as binding groups and indeed saw preferential oxidation of a substrate that coutd coordinate to the two metal ions arid span the porphyrin unit.