Iron(II)- and 2-(oxo)-glutarate-(Fe/2OG)-dependent oxygenases perform diverse transformations of unactivated C-H bonds. The range of possible chemistry in this enzyme platform suggests that catalytic activities can be reprogrammed by mutagenesis or use of substrate analogs. In this work, we show that Fe/2OG amino acid hydroxylase SadA can be converted to a halogenase by a single active site substitution. Substrate scope investigation shows that product partition and extent of turnover can be modulated based on side chain identity. The work suggests that Fe/2OG reprogramming can be exploited to install useful functional groups at inert aliphatic sites.

Reprogramming an iron(II)- and 2-(oxo)-glutarate-dependent hydroxylase to halogenate aliphatic N-succinyl-L-amino acids

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.