A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase

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Abstract

By constructing an in vivo-assembled, catalytically proficient peroxidase, C45, we have recently demonstrated the catalytic potential of simple, de novo-designed heme proteins. Here, we show that C45’s enzymatic activity extends to the efficient and stereoselective intermolecular transfer of carbenes to olefins, heterocycles, aldehydes, and amines. Not only is this a report of carbene transferase activity
in a completely de novo protein, but also of enzyme-catalyzed ring expansion of aromatic heterocycles via carbene transfer by any enzyme.
Original languageEnglish
Pages (from-to)1419-1428
Number of pages10
JournalProceedings of the National Academy of Sciences of the United States of America
Volume117
Issue number3
Early online date2 Jan 2020
DOIs
Publication statusPublished - 21 Jan 2020

Keywords

  • de novo protein design
  • enzyme design
  • carbene transfer
  • biocatalytic ring expansion
  • biocatalysis

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