Author: Prier, C.K.; Zhang, R.K.; Buller, A.R.; Brinkmann-Chen, S.; Arnold, F.H.
Description: C-H bonds are ubiquitous structural units of organic molecules. Although these bonds are generally considered to be chemically inert, the recent emergence of methods for C-H functionalization promises to transform the way synthetic chemistry is performed. The intermolecular amination of C-H bonds represents a particularly desirable and challenging transformation for which no efficient, highly selective, and renewable catalysts exist. Here we report the directed evolution of an iron-containing enzymatic catalyst-based on a cytochrome P450 monooxygenase-for the highly enantioselective intermolecular amination of benzylic C-H bonds. The biocatalyst is capable of up to 1,300 turnovers, exhibits excellent enantioselectivities, and provides access to valuable benzylic amines. Iron complexes are generally poor catalysts for C-H amination: in this catalyst, the enzyme’s protein framework confers activity on an otherwise unreactive iron-haem cofactor.
Subject headings:
Publication year: 2017
Journal or book title: Nature Chemistry
Volume: 9
Issue: 7
Pages: 629-634
Find the full text :Â https://www.nature.com/articles/nchem.2783
Find more like this one (cited by): https://scholar.google.com/scholar?cites=12450939709222528676&as_sdt=1000005&sciodt=0,16&hl=en
Type: Journal Article
Serial number: 2115