420088-65-9Relevant academic research and scientific papers
Catalytic oxidations of steroid substrates by artificial cytochrome p-450 enzymes.
Yang, Jerry,Gabriele, Bartolo,Belvedere, Sandro,Huang, Ying,Breslow, Ronald
, p. 5057 - 5067 (2002)
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.
Biomimetic hydroxylation of saturated carbons with artificial cytochrome P-450 enzymes - Liberating chemistry from the tyranny of functional groups
Breslow, Ronald,Yang, Jerry,Yan, Jiaming
, p. 653 - 659 (2007/10/03)
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
