Characterization of CuZnSOD model complexes from a redox point of view

Redox properties of copper(II) complexes of imidazole containing ligands

Sarolta Timári, Riccardo Cerea, K. Várnagy

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The systematic electrochemical studies of the copper complexes of various terminally protected tri-, tetra-, penta- and heptapeptides containing histidine in different location and number in the peptide chain and two histidine derivatives were carried out by cyclic voltammetry. The redox parameters of CuL and CuL2 complexes coordinating exclusively through imidazole nitrogens were determined. For all studied Cu(II) complexes the characteristic redox reactions are quasi-reversible one electron reduction processes. The obtained formal reduction potential values fall into the 200-400 mV potential range supporting the former results that the CuL and CuL2 complexes of these multihistidine peptides are not only structural but also good functional models of the Cu-Zn-superoxide dismutase (CuZnSOD) enzyme. These observations are confirmed by the results of SOD activity assay in a representative copper(II)-ligand system.

Original languageEnglish
Pages (from-to)1009-1017
Number of pages9
JournalJournal of Inorganic Biochemistry
Volume105
Issue number8
DOIs
Publication statusPublished - Aug 2011

Fingerprint

Histidine
Oxidation-Reduction
Copper
Ligands
Peptides
Rubiaceae
Redox reactions
Cyclic voltammetry
Assays
Nitrogen
Electrons
Derivatives
Enzymes
imidazole
Superoxide Dismutase
Superoxide Dismutase-1

Keywords

  • Cyclic voltammetry
  • Electrochemical properties
  • Imidazole ring
  • Multihistidine peptides
  • SOD models

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Characterization of CuZnSOD model complexes from a redox point of view : Redox properties of copper(II) complexes of imidazole containing ligands. / Timári, Sarolta; Cerea, Riccardo; Várnagy, K.

In: Journal of Inorganic Biochemistry, Vol. 105, No. 8, 08.2011, p. 1009-1017.

Research output: Contribution to journalArticle

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