Catalytic oxidations of steroid substrates by artificial cytochrome p-450 enzymes.
Catalysts comprising manganese-porphyrins carrying cyclodextrin binding groups are able to perform hydroxylations with substrate selectivity and regio- and stereoselectivity and high catalytic turnovers. The geometries of the catalyst/substrate complexes override intrinsic substrate reactivities, permitting attack on geometrically accessible saturated carbons of steroids in the presence of secondary carbinol groups and carbon-carbon double bonds, as in enzymatic reactions. Selective hydroxylations of steroid carbon 9 positions are of particular practical interest.
Department of Chemistry, Columbia University, New York, New York 10027, USA.
Jerry
J
Yang
Bartolo
B
Gabriele
Sandro
S
Belvedere
Ying
Y
Huang
Ronald
R
Breslow
D001665:Binding Sites; D002384:Catalysis; D003505:Cyclodextrins; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006900:Hydroxylation; D008345:Manganese; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011166:Porphyrins; D013237:Stereoisomerism; D013256:Steroids / Q000737:chemistry; D013379:Substrate Specificity
D003505:Cyclodextrins; D011166:Porphyrins; D013256:Steroids; D008345:Manganese; D003577:Cytochrome P-450 Enzyme System