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, pe...

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Bibliographic Details
Published in:Journal of organic chemistry 2002-07, Vol.67 (15), p.5057-5067
Main Authors: Yang, Jerry, Gabriele, Bartolo, Belvedere, Sandro, Huang, Ying, Breslow, Ronald
Format: Article
Language:English
Subjects:
Alicyclic compounds, terpenoids, prostaglandins, steroids
Binding Sites
Catalysis
Catalysts: preparations and properties
Chemistry
Cyclodextrins
Cytochrome P-450 Enzyme System - metabolism
Exact sciences and technology
General and physical chemistry
Hydroxylation
Manganese
Models, Molecular
Molecular Conformation
Molecular Structure
Organic chemistry
Oxidation-Reduction
Porphyrins
Preparations and properties
Stereoisomerism
Steroids
Steroids - chemistry
Substrate Specificity
Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry
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Summary: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.
ISSN:0022-3263
1520-6904
DOI:10.1021/jo020174u