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Communication
Selective Hydroxylation of a Steroid at C-9 by an Artificial Cytochrome P-450
Article first published online: 2 AUG 2000
DOI: 10.1002/1521-3773(20000804)39:15<2692::AID-ANIE2692>3.0.CO;2-3
© 2000 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany
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Additional Information
How to Cite
Yang, J. and Breslow, R. (2000), Selective Hydroxylation of a Steroid at C-9 by an Artificial Cytochrome P-450 . Angewandte Chemie International Edition, 39: 2692–2695. doi: 10.1002/1521-3773(20000804)39:15<2692::AID-ANIE2692>3.0.CO;2-3
Publication History
- Issue published online: 2 AUG 2000
- Article first published online: 2 AUG 2000
- Manuscript Received: 2 MAR 2000
- Abstract
- Cited By
Keywords:
- cyclodextrins;
- enzyme mimetics;
- oxidations;
- porphyrinoids;
- steroids
Graphical Abstract
A mimic of monooxygenase enzymes: An artificial cytochrome P-450 with four cyclodextrins linked to a manganese/porphyrin complex can insert an oxygen atom into unactivated C−H bonds with catalytic turnovers (see picture). Hydroxylation of a doubly bound diester of androstane-3,17-diol at C-6 is possible; further oxidation of the triply bound triester of this product occurs at C-9.