In this section
@article{Craven:2021:10.1038/s41929-021-00603-3,
author = {Craven, EJ and Latham, J and Shepherd, SA and Khan, I and Diaz-Rodriguez, A and Greaney, MF and Micklefield, J},
doi = {10.1038/s41929-021-00603-3},
journal = {NATURE CATALYSIS},
pages = {385--394},
title = {Programmable late-stage C-H bond functionalization enabled by integration of enzymes with chemocatalysis},
url = {http://dx.doi.org/10.1038/s41929-021-00603-3},
volume = {4},
year = {2021}
}
TY - JOUR
AB - New chemo- and biocatalytic methodology is important for the future sustainable synthesis of essential molecules. Transition metal catalysis enables the late-stage C-H functionalization of some complex molecular scaffolds, providing rapid routes to valuable products, although this is largely dependent on the availability of electronically or sterically predisposed C-H bonds for selective metalation, leaving certain regioselectivities inaccessible. Unlike metal chemocatalysis, enzymes can catalyse C-H bond functionalization, discriminating between near-identical, non-activated C-H bonds, delivering products with exquisite regioselectivity. However, enzymes typically provide access to fewer functionalities than more divergent chemocatalysis. Here we report programmable, regioselective C-H bond functionalization methodologies for the installation of versatile nitrile, amide and carboxylic acid moieties through integration of halogenase enzymes with palladium-catalysed cyanation and subsequent incorporation of nitrile hydratase or nitrilase enzymes. Using two- or three-component chemobiocatalytic systems, the regioselective synthesis of complex target molecules, including pharmaceuticals, can be achieved in a one-pot process operable on a gram scale.
AU - Craven,EJ
AU - Latham,J
AU - Shepherd,SA
AU - Khan,I
AU - Diaz-Rodriguez,A
AU - Greaney,MF
AU - Micklefield,J
DO - 10.1038/s41929-021-00603-3
EP - 394
PY - 2021///
SN - 2520-1158
SP - 385
TI - Programmable late-stage C-H bond functionalization enabled by integration of enzymes with chemocatalysis
T2 - NATURE CATALYSIS
UR - http://dx.doi.org/10.1038/s41929-021-00603-3
VL - 4
ER -