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|Title:||HOW THE A-HUDROXYMETHYLSERINE RESIDUE STABILIZES OLIGOPEPTIDE COMPLEXES WITH NICKEL(II) AND COPPER(II) IONS||Authors:||Mlynarz, P
|Issue Date:||2000||Project:||None||Journal:||JOURNAL OF THE CHEMICAL SOCIETY DALTON TRANSACTIONS||Abstract:||
Potentiometric, spectroscopic and theoretical studies have shown that the alpha-hydroxymethylserine (HmS) residue is a very specific amino acid residue when inserted into a peptide sequence. The theoretical calculations as well as evaluated deprotonation microconstants indicated that in the HmS-HmS-His tripeptide the N-terminal ammonium group is more acidic than the imidazole nitrogen. The hydrogen bond formation between the N-terminal amino group and imidazole nitrogen stabilizes the cyclic conformation of the metal-free peptide. The unusual gain in the 4N complex stability in the copper(II) and nickel(II) complexes with HmS-HmS-His ligands seems to derive from the enhancement of the pi-electron contribution to the metal-amide nitrogen bond.
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