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Transition‐Metal Catalysis as a Tool for the Covalent Labeling of Proteins
Author(s) -
van Maarseveen Jan H.,
Reek Joost N. H.,
Back Jaap Willem
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200504352
Subject(s) - chemistry , amination , covalent bond , catalysis , lysine , tryptophan , transition metal , alkylation , reductive amination , aqueous solution , combinatorial chemistry , posttranslational modification , organic chemistry , amino acid , biochemistry , enzyme
They make a good couple : Protein modification the transition‐metal catalysis enables the selective labeling of proteins and has been demonstrated in complex mixtures. Current examples of such coupling reactions are the Ir‐catalyzed reductive amination of lysine residues and the alkylation of tryptophan residues by Rh carbenes in proteins under aqueous conditions (see scheme).