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We describe palladium-mediated S-arylation that exploits natural metal-binding motifs to ensure high site selectivity for a proximal reactive residue. This allows the chemical identification not only of proteins that bind metals but also the environment of the metal-binding site itself through proteomic analysis of arylation sites. The transformation is easy to perform under standard conditions, does not require the isolation of a reactive Ar-Pd complex, is broad in scope, and is applicable in cell lysates as well as to covalent inhibition/modulation of metal-dependent enzymatic activity.

Original publication

DOI

10.1021/jacs.6b04043

Type

Journal article

Journal

J Am Chem Soc

Publication Date

20/07/2016

Volume

138

Pages

8678 - 8681

Keywords

Binding Sites, Catalysis, Hydrocarbons, Aromatic, Mannosyltransferases, Models, Molecular, Palladium, Protein Conformation, Rhodothermus