Voltammetric study of the interaction between oxacillin sodium and cysteine in the presence and absence of Mn(II) ions in neutral buffer solution

Bicer E., Coskun E.

JOURNAL OF THE SERBIAN CHEMICAL SOCIETY, vol.72, no.10, pp.1003-1013, 2007 (SCI-Expanded) identifier

  • Publication Type: Article / Article
  • Volume: 72 Issue: 10
  • Publication Date: 2007
  • Doi Number: 10.2298/jsc0710003b
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1003-1013
  • Keywords: voltammetry, oxacillin, cysteine, interaction, BINDING PROTEIN 2A, PENICILLIN, MECHANISM, ANTIBIOTICS, AUREUS
  • Ondokuz Mayıs University Affiliated: Yes


In this study, the voltammetric behaviour of the interaction of oxacillin sodium (OXA) and OXA-cysteine (RSH) was studied by square-wave voltammetry, cyclic voltammetry in Britton-Robinson (B-R) buffer (pH 7.0). OXA gave two peaks at -0.248 and -1.224 V. For the interaction, the peak of mercurous cysteine thiolate (Hg-2(SR)(2)) was selected. It was found that the peak currents corresponding to Hg-2(SR)(2) significantly decreased, while the peak potential shifted to more positive potentials upon the addition of OXA. The observed phenomena are due to the interaction of OXA with RSH on the surface of the mercury electrode. When OXA was added to the electrochemical cell along with Mn(II), new peaks at -0.146 and -0.608 V were observed. These peaks were due to the catalytic activity of OXA on the reduction of Mn(II) and could be attributed to the formation of Mn(II) complexes with different metal/ligand ratios. On the other hand, in the presence of RSH, the peak at -0.608 V vanished and a reduction peak was observed at-0.662 V. The catalytic reduction peak potential of Mn(II) at-0.662 V indicated that RSH slightly prevented the catalysis process of OXA due to their mutual interaction.