Highly specific oxidative cross-linking of proteins mediated by a nickel-peptide complex.
The Ni(II) complex of the tripeptide NH2-Gly-Gly-His-COOH is shown to mediate efficient protein-protein cross-linking in the presence of oxidants such as oxone and monoperoxyphthalic acid. Only proteins that associate specifically in solution are cross-linked under these conditions. Preliminary probes of the mechanism of the reaction suggest that the active intermediate may be a high-valent metal complex that attacks aromatic amino acids.
Brown
K C
KC
Department of Chemistry and Biochemistry, University of Texas at Austin 78712-1096, USA.
Yang
S H
SH
Kodadek
T
T
D000085:Acetates / Q000737:chemistry; D019342:Acetic Acid; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D003432:Cross-Linking Reagents / Q000737:chemistry*; D008969:Molecular Sequence Data; D009532:Nickel / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D016877:Oxidants / Q000737:chemistry*; D010084:Oxidation-Reduction; D010795:Phthalic Acids / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*
D000085:Acetates; D000596:Amino Acids; D003432:Cross-Linking Reagents; D009842:Oligopeptides; D016877:Oxidants; D010795:Phthalic Acids; D011506:Proteins; C037026:diglycyl-histidine; D009532:Nickel; C063907:monoperoxyphthalate; D019342:Acetic Acid