| Autor: |
GuangRong Peh, Terence Tay, Lee Ling Tan, Elaine Tiong, Jiawu Bi, Yi Ling Goh, Suming Ye, Fu Lin, Cheryl Jia Xin Tan, Yong Zi Tan, Joel Wong, Huimin Zhao, Fong Tian Wong, Ee Lui Ang, Yee Hwee Lim |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
|
| Zdroj: |
Communications Chemistry, Vol 7, Iss 1, Pp 1-9 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2399-3669 |
| DOI: |
10.1038/s42004-023-01083-1 |
| Popis: |
Abstract Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole halogenation in organic synthesis, corresponding reports on enzymatic pyrrole halogenation have been lacking. Here we describe the in vitro functional and structural characterization of PrnC, a flavin-dependent halogenase that can act on free-standing pyrroles. Computational modeling and site mutagenesis studies identified three key residues in the catalytic pocket. A moderate resolution map using single-particle cryogenic electron microscopy reveals PrnC to be a dimer. This native PrnC can halogenate a library of structurally diverse pyrrolic heterocycles in a site-selective manner and be applied in the chemoenzymatic synthesis of a chlorinated analog of the agrochemical fungicide Fludioxonil. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
|
Nepřihlášeným uživatelům se plný text nezobrazuje |
K zobrazení výsledku je třeba se přihlásit.
|
