Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4477
Title: HOW THE A-HUDROXYMETHYLSERINE RESIDUE STABILIZES OLIGOPEPTIDE COMPLEXES WITH NICKEL(II) AND COPPER(II) IONS
Authors: Mlynarz, P
Gaggelli, Nicola 
Panek, J
Stasiak, M
Valensin, Gianni 
Kowalik, T
Leplawi, M
Lataika, Z
Kozlowski, H.
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.
Description: 
183909
URI: http://hdl.handle.net/20.500.12779/4477
ISSN: 0300-9246
DOI: 10.1039/a909354k
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