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New-to-nature chemistry from old protein machinery: carbene and nitrene transferases

Liu, Zhen and Arnold, Frances H. (2021) New-to-nature chemistry from old protein machinery: carbene and nitrene transferases. Current Opinion in Biotechnology, 69 . pp. 43-51. ISSN 0958-1669. https://resolver.caltech.edu/CaltechAUTHORS:20210104-164231981

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Abstract

Hemoprotein-catalyzed carbene and nitrene transformations have emerged as powerful tools for constructing complex molecules; they also nicely illustrate how new protein catalysts can emerge, evolve and diversify. These laboratory-invented enzymes exploit the ability of proteins to tame highly reactive carbene and nitrene species and direct their fates with high selectivity. New-to-nature carbene and nitrene transferases catalyze many useful reactions, including some that have no precedent using chemical methods. Here we cover recent advances in this field, including alkyne cyclopropenation, arene cyclopropanation, carbene Csingle bondH insertion, intramolecular nitrene Csingle bondH insertion, alkene aminohydroxylation, and primary amination. For such transformations, biocatalysts have exceeded the performance of reported small-molecule catalysts in terms of selectivity and catalyst turnovers. Finally, we offer our thoughts on using these new enzymatic reactions in chemical synthesis, integrating them into biological pathways and chemo-enzymatic cascades, and on their current limitations.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1016/j.copbio.2020.12.005DOIArticle
ORCID:
AuthorORCID
Liu, Zhen0000-0002-6313-823X
Arnold, Frances H.0000-0002-4027-364X
Additional Information:© 2020 Elsevier. Available online 25 December 2020. This work was supported by the NSF Division of Molecular and Cellular Biosciences (2016137), the NIH National Institute of General Medical Sciences (R01GM138722), the U.S. Department of Energy (DE-SC0021141), the US Army Research Office Institute for Collaborative Biotechnologies (cooperative agreement W911NF-19-2-0026 and contract W911NF-19-D-0001), and the Jacobs Institute for Molecular Engineering for Medicine at Caltech. The content is solely the responsibility of the authors and does not necessarily represent the official views of the funding agencies. The authors thank Dr Benjamin Levin, Dr Sabine Brinkmann-Chen, Dr Kai Chen, Dr Yang Yang, Dr David Miller, and Dr Soumitra Athavale for helpful discussions and comments on the manuscript. Conflict of interest statement. Nothing declared.
Group:Jacobs Institute for Molecular Engineering for Medicine
Funders:
Funding AgencyGrant Number
NSFMCB-2016137
NIHR01GM138722
Department of Energy (DOE)DE-SC0021141
Army Research Office (ARO)W911NF-19-2-0026
Army Research Office (ARO)W911NF-19-D-0001
Joseph J. Jacobs Institute for Molecular Engineering for MedicineUNSPECIFIED
Record Number:CaltechAUTHORS:20210104-164231981
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20210104-164231981
Official Citation:Zhen Liu, Frances H Arnold, New-to-nature chemistry from old protein machinery: carbene and nitrene transferases, Current Opinion in Biotechnology, Volume 69, 2021, Pages 43-51, ISSN 0958-1669, https://doi.org/10.1016/j.copbio.2020.12.005.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:107311
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:05 Jan 2021 15:29
Last Modified:05 Jan 2021 15:29

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