2000
DOI: 10.1039/a907342f
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Equilibrium and structural studies on copper(II) complexes of tetra-, penta- and hexa-peptides containing histidyl residues at the C-termini

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Cited by 90 publications
(129 citation statements)
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“…The EPR parameters (g k = 2.226 and A k = 162 10 À4 cm À1 ) are very similar to those reported for both the Cu 2 + complexes of Gly 5 His peptides and some Ab peptide fragments supporting the same (NH 2 , N À , N Im ) coordination mode. [37][38][39] These parameters are indicative of the presence of three nitrogen donor atoms in a highly distorted environment. This distortion from square-planar or pseudo-octahedral geometry is ascribable to the presence of an apical oxygen atom (e.g., a carboxylate) or an imidazole nitrogen atom.…”
Section: A C H T U N G T R E N N U N G [Cul]mentioning
confidence: 99%
“…The EPR parameters (g k = 2.226 and A k = 162 10 À4 cm À1 ) are very similar to those reported for both the Cu 2 + complexes of Gly 5 His peptides and some Ab peptide fragments supporting the same (NH 2 , N À , N Im ) coordination mode. [37][38][39] These parameters are indicative of the presence of three nitrogen donor atoms in a highly distorted environment. This distortion from square-planar or pseudo-octahedral geometry is ascribable to the presence of an apical oxygen atom (e.g., a carboxylate) or an imidazole nitrogen atom.…”
Section: A C H T U N G T R E N N U N G [Cul]mentioning
confidence: 99%
“…The wavelength region of the systematic deviations of the residual intensities is between 600 and 700 nm which gives rise for speculation that the stoichiometry of the new species is rather CuL (with NH 2 and ImN in the coordination sphere) than CuHL (1N coordination). Recently, several peptides have been suggested to complex copper(II) ions by both the N-terminal amine and the imidazole group of a farther histidine within a macrochelate loop [31,48] in the peptides with the histidine in position n > 3 from the N-terminus. Based on the above considerations we suppose a macrochelate type coordination to appear in the CuL complex as shown in Scheme 1.…”
Section: Copper(ii)-xaa-xaa-his Systemsmentioning
confidence: 99%
“…The metal binding features of oligopeptides, including the effect of the number and position of histidine residues within the peptide chain have been summarized in a couple of reviews within the last decade [1,9,10]. There have been a number of systematic studies attempting to explore the role of the terminal amino group and a histidine at the fourth or higher position in the peptide sequence, as primary coordination sites for copper(II) and nickel(II) [11][12][13][14][15][16]. However, the obtained results were sometimes contradictory and generated some debates.…”
Section: Introductionmentioning
confidence: 99%