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


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.

SUBMITTER: Stenner R 

PROVIDER: S-EPMC6983366 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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

Stenner Richard R   Steventon Jack W JW   Seddon Annela A   Anderson J L Ross JLR  

Proceedings of the National Academy of Sciences of the United States of America 20200102 3


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 he  ...[more]

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