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Integrated catalysis opens new arylation pathways via regiodivergent enzymatic C–H activation

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Latham, Jonathan, Henry, Jean-Marc, Sharif, Humera H., Menon, Binuraj R. K., Shepherd, Sarah A., Greaney, Michael F. and Micklefield, Jason (2016) Integrated catalysis opens new arylation pathways via regiodivergent enzymatic C–H activation. Nature Communications, 7 . 11873. doi:10.1038/ncomms11873

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Official URL: http://dx.doi.org/10.1038/ncomms11873

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Abstract

Despite major recent advances in C–H activation, discrimination between two similar, unactivated C–H positions is beyond the scope of current chemocatalytic methods. Here we demonstrate that integration of regioselective halogenase enzymes with Pd-catalysed cross-coupling chemistry, in one-pot reactions, successfully addresses this problem for the indole heterocycle. The resultant ‘chemobio-transformation’ delivers a range of functionally diverse arylated products that are impossible to access using separate enzymatic or chemocatalytic C–H activation, under mild, aqueous conditions. This use of different biocatalysts to select different C–H positions contrasts with the prevailing substrate-control approach to the area, and presents opportunities for new pathways in C–H activation chemistry. The issues of enzyme and transition metal compatibility are overcome through membrane compartmentalization, with the optimized process requiring no intermediate work-up or purification steps.

Item Type: Journal Article
Divisions: Faculty of Science > Life Sciences (2010- )
Journal or Publication Title: Nature Communications
Publisher: Nature Publishing Group
ISSN: 2041-1723
Official Date: 10 June 2016
Dates:
DateEvent
10 June 2016Published
9 May 2016Accepted
Volume: 7
Article Number: 11873
DOI: 10.1038/ncomms11873
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access

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