Jiaming Yan

Biomimetic hydroxylation of saturated carbons with artificial cytochrome P-450 enzymes—liberating chemistry from the tyranny of functional groups

Abstract Five mimics of cytochrome P-450 have been prepared and examined as catalysts for the specific hydroxylation of steroids. Reactions occur dictated by the geometries of the complexes, overcoming the intrinsic reactivity of a carbon–carbon double bond and of a secondary carbinol group. In some cases as many as 3000 catalytic turnovers are observed.

Catalytic hydroxylation of steroids by cytochrome P-450 mimics. Hydroxylation at C-9 with novel catalysts and steroid substrates

Double binding of a steroid substrate to our previously described mimic of the cytochrome P-450 enzymes hydroxylates carbon 9 of the steroid, but with a second significant product. The geometry has been adjusted with new catalysts that show high selectivity and excellent turnover for the C-9 hydroxylation.

An enzyme mimic that hydrolyzes an unactivated ester with catalytic turnover

Abstract The Cu(II) complex of a cyclodextrin dimer linked by a bipyridyl unit catalyzes the hydrolysis of an unactivated doubly-bound benzyl ester.