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Published August 26, 2013 | Accepted Version
Journal Article Open

Enantioselective Intramolecular C-H Amination Catalyzed by Engineered Cytochrome P450 Enzymes In Vitro and In Vivo

Abstract

Nitrogen activation: Though P450 enzymes are masters of oxygen activation and insertion into C-H 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 C-H aminations in azide substrates. Mutations to two highly conserved residues significantly increased this activity.

Additional Information

© 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Received: May 22, 2013; Revised: June 12, 2013; Published online: July 24, 2013. We thank S. Virgil and the 3CS catalysis center at Caltech for assistance with HPLC and LC–MS analyses, and D. Montgomery, Y. Liu, N. Peck, K. Rabe, R. Lauchli, and D. VanderVelde for helpful discussions. This work was supported by the Department of the Navy, Office of Naval Research (grant N00014-11-1-0205), and by the Jacobs Institute for Molecular Engineering for Medicine at Caltech. J.A.M. and Z.J.W. are supported by Ruth L. Kirschstein National Research Service Awards (F32GM101792) and (F32EB015846). C.C.F. is supported by an NSF Graduate Research Fellowship.

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Created:
August 22, 2023
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October 24, 2023