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

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 carbene...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2020-01, Vol.117 (3), p.1419-1428
Main Authors: Stenner, Richard, Steventon, Jack W., Seddon, Annela, Anderson, J. L. Ross
Format: Article
Language:English
Subjects:
Aldehydes
Aldehydes - chemistry
Alkenes
Alkenes - chemistry
Amines
Amines - chemistry
Biocatalysis
Biological Sciences
Carbenes
Enzymatic activity
Enzymes
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Heme proteins
Heterocyclic compounds
Methane - analogs & derivatives
Methane - chemistry
Peroxidase
Peroxidases - chemistry
Peroxidases - metabolism
Proteins
Stereoselectivity
Substrate Specificity
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1915054117