Coordination, redox properties and SOD activity of Cu(II) complexes of multihistidine peptides

Gizella Csire, Sarolta Timári, József Asztalos, Judit Mária Király, Mariann Kiss, K. Várnagy

Research output: Contribution to journalArticle

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Abstract

The results of electrochemical and SOD activity measurements of such copper(II) complexes of terminally protected multihistidine peptides that may mimic the active site of CuZnSOD enzyme are submitted and completed with solution equilibrium studies of some copper(II)-ligand systems. The equilibrium data confirm that the thermodynamic stabilities increase with the increasing number of histidyl residues in the amino acid sequence, the stability order, however, can be finely tuned by the number and quality of amino acids between histidine residues. Based on the cyclic voltammetric studies we concluded that the formal reduction potential values of imidazole nitrogen coordinated complexes decrease with the increasing number of imidazole donor atoms in the coordination sphere. However, the redox parameters of [CuH−1L]+ and [CuH−2L] complexes containing amide nitrogen coordination can be determined as well. All formal potential values of [CuL]2+, [CuH−1L]+ and [CuH−2L] complexes fall in the middle potential range of SOD activity. Finally, after the detailed analysis of species distribution curves based upon the equilibrium data SOD activity of copper(II) containing systems at two pH (pH = 6.8 and 7.4) were determined. The imidazole coordinated [CuL]2+ complexes of the multihistidine peptide containing the HXH sequence exhibit the most significant activity, but the presence of amide nitrogen coordinated species with slightly distorted geometry could considerably contribute to the SOD activity.

Original languageEnglish
Pages (from-to)198-210
Number of pages13
JournalJournal of Inorganic Biochemistry
Volume177
DOIs
Publication statusPublished - Dec 1 2017

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Oxidation-Reduction
Copper
Nitrogen
Amides
Peptides
Amino Acids
Thermodynamics
Histidine
Amino Acid Sequence
Catalytic Domain
Thermodynamic stability
Ligands
Atoms
Geometry
Enzymes
imidazole

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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Coordination, redox properties and SOD activity of Cu(II) complexes of multihistidine peptides. / Csire, Gizella; Timári, Sarolta; Asztalos, József; Király, Judit Mária; Kiss, Mariann; Várnagy, K.

In: Journal of Inorganic Biochemistry, Vol. 177, 01.12.2017, p. 198-210.

Research output: Contribution to journalArticle

Csire, Gizella ; Timári, Sarolta ; Asztalos, József ; Király, Judit Mária ; Kiss, Mariann ; Várnagy, K. / Coordination, redox properties and SOD activity of Cu(II) complexes of multihistidine peptides. In: Journal of Inorganic Biochemistry. 2017 ; Vol. 177. pp. 198-210.
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