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Exploring the Biocatalytic Potential of Fe/α‐Ketoglutarate‐Dependent Halogenases
Author(s) -
Voss Moritz,
Honda Malca Sumire,
Buller Rebecca
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201905752
Subject(s) - regioselectivity , directed evolution , halogenation , enzyme , protein engineering , chemistry , substrate (aquarium) , indole test , stereochemistry , combinatorial chemistry , biochemistry , organic chemistry , catalysis , biology , ecology , mutant , gene
Abstract Freestanding Fe/α‐ketoglutarate‐dependent halogenases are oxidoreductases that catalyze the installation of halogen atoms into unactivated sp 3 ‐hybridized carbon centers with high stereo‐ and regioselectivity. Since their discovery in 2014, a small number of indole alkaloid and amino acid halogenases have been identified and characterized. First enzyme engineering examples suggest that the accessible substrate range of these enzymes may be expanded through the use of rational enzyme design and directed evolution. Structural investigations of non‐heme iron halogenases acting on freestanding as well as tethered substrates are beginning to inform about the principles of the underlying halogenation mechanism.