Highly specific oxidative cross-linking of proteins mediated by a nickel-peptide complex.
K C Brown, S H Yang, T Kodadek
Index: Biochemistry 34(14) , 4733-9, (1995)
Full Text: HTML
Abstract
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.
Related Compounds
Related Articles:
2009-06-01
[J. Inorg. Biochem. 103 , 871-875, (2009)]
2012-01-01
[Acta Pol. Pharm. 69(6) , 1303-6, (2012)]
Diastereoselective DNA cleavage recognition by Ni(II) x Gly-Gly-His-derived metallopeptides.
2006-03-15
[J. Am. Chem. Soc. 128(10) , 3198-207, (2006)]
Generation of free radicals from lipid hydroperoxides by Ni2+ in the presence of oligopeptides.
1992-11-15
[Arch. Biochem. Biophys. 299(1) , 154-62, (1992)]
Protein cross-linking mediated by metal ion complexes.
2001-01-01
[Met. Ions Biol. Syst. 38 , 351-84, (2001)]