The influence of aspartic or glutamic acid residues in tetrapeptides on the formation of complexes with nickel(II) and zinc(II)
Identifieur interne : 000474 ( France/Analysis ); précédent : 000473; suivant : 000475The influence of aspartic or glutamic acid residues in tetrapeptides on the formation of complexes with nickel(II) and zinc(II)
Auteurs : H. Kozlowski [Pologne] ; A. Lebkiri [Maroc] ; Ch. O. Onindo [Royaume-Uni] ; L. D. Pettit [Royaume-Uni] ; J.-F. Galey [France]Source :
- Polyhedron [ 0277-5387 ] ; 1995.
Abstract
The formation of the complexes formed by NiII and ZnII with Asp-Asp-Asp and a series of tetrapeptides containing one or two Asp residues or one Glu residue are reported. Stability constants were measured pH-metrically. The particular species and the metal ion binding sites were determined using 1H NMR, UV-vis and CD spectroscopy. The β-carboxylate group of the Asp residue stabilizes the complexes significantly, particularly when present as the N-terminal residue. As a result the tendency for NiII to deprotonate and bind to amide-nitrogen atoms, forming planar diamagnetic complexes, is reduced and their formation delayed to a significantly higher pH when compared to other peptides. The side chain of the Glu residue has a much smaller effect. As anticipated, ZnII was unable to deprotonate and bind to peptide nitrogens.
Url:
DOI: 10.1016/0277-5387(94)00239-B
Affiliations:
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<front><div type="abstract" xml:lang="en">The formation of the complexes formed by NiII and ZnII with Asp-Asp-Asp and a series of tetrapeptides containing one or two Asp residues or one Glu residue are reported. Stability constants were measured pH-metrically. The particular species and the metal ion binding sites were determined using 1H NMR, UV-vis and CD spectroscopy. The β-carboxylate group of the Asp residue stabilizes the complexes significantly, particularly when present as the N-terminal residue. As a result the tendency for NiII to deprotonate and bind to amide-nitrogen atoms, forming planar diamagnetic complexes, is reduced and their formation delayed to a significantly higher pH when compared to other peptides. The side chain of the Glu residue has a much smaller effect. As anticipated, ZnII was unable to deprotonate and bind to peptide nitrogens.</div>
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