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

Richard Stenner; Jack W. Steventon; Annela Seddon; J. L. Ross Anderson

doi:10.1073/pnas.1915054117

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

Richard Stenner, Jack W. Steventon, Annela Seddon, J. L. Ross Anderson

Research output: Contribution to journal › Article (Academic Journal) › peer-review

66 Citations (Scopus)

215 Downloads (Pure)

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 language	English
Pages (from-to)	1419-1428
Number of pages	10
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	117
Issue number	3
Early online date	2 Jan 2020
DOIs	https://doi.org/10.1073/pnas.1915054117
Publication status	Published - 21 Jan 2020

Research Groups and Themes

Bristol BioDesign Institute

Keywords

synthetic biology
biocatalysis
de novo protein design
enzyme design
carbene transfer
biocatalytic ring expansion

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10.1073/pnas.1915054117

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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.
Final published version, 1.18 MBLicence: CC BY-NC-ND

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title = "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{\textquoteright}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.",

keywords = "synthetic biology, biocatalysis, de novo protein design, enzyme design, carbene transfer, biocatalytic ring expansion",

author = "Richard Stenner and Steventon, \{Jack W.\} and Annela Seddon and Anderson, \{J. L. Ross\}",

year = "2020",

month = jan,

day = "21",

doi = "10.1073/pnas.1915054117",

language = "English",

volume = "117",

pages = "1419--1428",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

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TY - JOUR

T1 - A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase

AU - Stenner, Richard

AU - Steventon, Jack W.

AU - Seddon, Annela

AU - Anderson, J. L. Ross

PY - 2020/1/21

Y1 - 2020/1/21

N2 - 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.

AB - 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.

KW - synthetic biology

KW - biocatalysis

KW - de novo protein design

KW - enzyme design

KW - carbene transfer

KW - biocatalytic ring expansion

UR - https://www.scopus.com/pages/publications/85078163542

U2 - 10.1073/pnas.1915054117

DO - 10.1073/pnas.1915054117

M3 - Article (Academic Journal)

C2 - 31896585

SN - 0027-8424

VL - 117

SP - 1419

EP - 1428

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 3

ER -

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

Abstract

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Construction of catalytically proficient enzymes from de novo designed proteins

Professor J L R Anderson

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

Abstract

Research Groups and Themes

Keywords

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Construction of catalytically proficient enzymes from de novo designed proteins

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Professor J L R Anderson

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