نبذة مختصرة : 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. ; © 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. ; Accepted Version - nihms-1658024.pdf
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