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Structure-guided reprogramming of a hydroxylase to halogenate its small molecule substrate.

著者 Mitchell AJ , Dunham NP , Bergman JA , Wang B , Zhu Q , Chang WC , Liu X , Boal AK
Biochemistry.2016 Dec 28 ; ():.
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Enzymatic installation of chlorine/bromine upon unactivated carbon centers provides a more versatile, selective, and environmentally-friendly alternative to chemical halogenation. Iron(II)- and 2-(oxo)-glutarate (FeII/2OG)-dependent halogenases are powerful biocatalysts that are capable of cleaving aliphatic C-H bonds to install useful functional groups, including halogens. Using a structure of the Fe/2OG halogenase, WelO5, in complex with its small-molecule substrate, we identified a similar N-acyl amino acid hydroxylase, SadA, and re-programmed it to halogenate its substrate, thereby gen-erating a new chiral haloalkyl center. The work highlights the potential of FeII/2OG enzymes as platforms for development of novel stereospecific catalysts for late-stage C-H functionalization.
PMID: 28029241 [PubMed - as supplied by publisher]
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