title: Selective Metal-Site-Guided Arylation of Proteins.
abstract: 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.
authors.affiliation: Department of Chemistry, Chemistry Research Laboratory, University of Oxford , Mansfield Road, Oxford OX1 3TA, U.K.
authors.forename: Jens
authors.initials: J
authors.lastname: Willwacher
authors.affiliation: Department of Chemistry, Chemistry Research Laboratory, University of Oxford , Mansfield Road, Oxford OX1 3TA, U.K.
authors.forename: Ritu
authors.initials: R
authors.lastname: Raj
authors.affiliation: Department of Chemistry, Chemistry Research Laboratory, University of Oxford , Mansfield Road, Oxford OX1 3TA, U.K.
authors.forename: Shabaz
authors.initials: S
authors.lastname: Mohammed
authors.affiliation: Department of Chemistry, Chemistry Research Laboratory, University of Oxford , Mansfield Road, Oxford OX1 3TA, U.K.
authors.forename: Benjamin G
authors.initials: BG
authors.lastname: Davis
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D006841:Hydrocarbons, Aromatic / Q000737:chemistry; D008364:Mannosyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010165:Palladium / Q000737:chemistry*; D011487:Protein Conformation; D045245:Rhodothermus / Q000201:enzymology
chemical_list: D006841:Hydrocarbons, Aromatic; D010165:Palladium; D008364:Mannosyltransferases; C402687:mannosylglycerate synthase