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

Research output: Contribution to journalArticle

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
DOIs
DateAccepted/In press - 10 Dec 2019
DatePublished (current) - 2 Jan 2020

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.

    Research areas

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

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    Rights statement: This is the final published version of the article (version of record). It first appeared online via National Academy of Sciences at https://www.pnas.org/content/117/3/1419 . Please refer to any applicable terms of use of the publisher.

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    Licence: CC BY-NC-ND

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