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Enantioselective Intramolecular CH Amination Catalyzed by Engineered Cytochrome P450 Enzymes In Vitro and In Vivo
Author(s) -
McIntosh John A.,
Coelho Pedro S.,
Farwell Christopher C.,
Wang Z. Jane,
Lewis Jared C.,
Brown Tristan R.,
Arnold Frances H.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201304401
Subject(s) - amination , intramolecular force , chemistry , enantioselective synthesis , enzyme , in vivo , cytochrome p450 , azide , catalysis , in vitro , stereochemistry , biochemistry , organic chemistry , biology , microbiology and biotechnology
Nitrogen activation : Though P450 enzymes are masters of oxygen activation and insertion into CH bonds, their ability to use nitrogen for the same purpose has so far not been explored. Engineered variants of cytochrome P450 BM3 have now been found to catalyze intramolecular CH aminations in azide substrates. Mutations to two highly conserved residues significantly increased this activity.