Biomimetic oxidation of unactivated carbons in steroids by a model of cytochrome P-450, oxorutheniumporphyrinate complex.
Biomimetic oxidation of unactivated carbons for structurally different steroids was studied with a model of cytochrome P-450, oxorutheniumporphyrinate complex, which is generated in situ by 2,6-dichloropyridine N-oxide as an oxygen donor and (5,10,15,20-tetramesitylporphyrinate) ruthenium(II) carbonyl complex and HBr as catalysts. The O-insertion positions depended significantly on specific structural features of the substrates to give novel and remote-oxygenated steroids in one step. The electrophilic oxorutheniumporphyrinate attacked predominantly allylic and benzylic beta-carbons adjacent to a pi-bond and/or less hindered, electron-rich tert-methine carbons in the substrates to give regio- and stereoselectively the corresponding oxo and/or hydroxy derivatives.
Lida
Takashi
T
Department of Chemistry, College of Humanities and Sciences, Nihon University, Sakurajousui, Setagaya, Tokyo 156-8550, Japan. takaiida@chs.nihon-u.ac.jp
Ogawa
Shoujiro
S
Miyata
Shouhei
S
Goto
Takaaki
T
Mano
Nariyasu
N
Goto
Junichi
J
Nambara
Toshio
T
D032701:Biomimetics; D002244:Carbon / Q000737:chemistry / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D009942:Organometallic Compounds / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism; D017975:Ruthenium Compounds / Q000737:chemistry / Q000378:metabolism*; D013256:Steroids / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D009942:Organometallic Compounds; D011166:Porphyrins; D017975:Ruthenium Compounds; D013256:Steroids; D002244:Carbon; D003577:Cytochrome P-450 Enzyme System