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- Title
Directed Evolution of an Iron(II)‐ and α‐Ketoglutarate‐Dependent Dioxygenase for Site‐Selective Azidation of Unactivated Aliphatic C−H Bonds**.
- Authors
Gomez, Christian A.; Mondal, Dibyendu; Du, Qian; Chan, Natalie; Lewis, Jared C.
- Abstract
FeII‐ and α‐ketoglutarate‐dependent halogenases and oxygenases can catalyze site‐selective functionalization of C−H bonds via a variety of C−X bond forming reactions, but achieving high chemoselectivity for functionalization using non‐native functional groups remains rare. The current study shows that directed evolution can be used to engineer variants of the dioxygenase SadX that address this challenge. Site‐selective azidation of succinylated amino acids and a succinylated amine was achieved as a result of mutations throughout the SadX structure. The installed azide group was reduced to a primary amine, and the succinyl group required for azidation was enzymatically cleaved to provide the corresponding amine. These results provide a promising starting point for evolving additional SadX variants with activity on structurally distinct substrates and for enabling enzymatic C−H functionalization with other non‐native functional groups.
- Subjects
AZIDATION; CHEMOSELECTIVITY; IRON; HALOGENASES; FUNCTIONAL groups; OXYGENASES; CARBON-hydrogen bonds
- Publication
Angewandte Chemie, 2023, Vol 135, Issue 15, p1
- ISSN
0044-8249
- Publication type
Academic Journal
- DOI
10.1002/ange.202301370