Nedzhib Ahmed, Stoykova Silviya, Atanasov Vasil, Pantcheva Ivayla, Antonov Liudmil
Laboratory of Biocoordination and Bioanalytical Chemistry, Department of Analytical Chemistry, Faculty of Chemistry and Pharmacy, "St. Kl. Ohridski" University of Sofia, Sofia, Bulgaria.
Laboratory of Biocoordination and Bioanalytical Chemistry, Department of Analytical Chemistry, Faculty of Chemistry and Pharmacy, "St. Kl. Ohridski" University of Sofia, Sofia, Bulgaria ; Emergency Toxicology Clinic, Military Medical Academy, Sofia, Bulgaria.
Interdiscip Toxicol. 2014 Sep;7(3):139-45. doi: 10.2478/intox-2014-0019. Epub 2014 Dec 30.
The ability of the acetylcholinesterase reactivator obidoxime (H2L(2+)) to bind palladium(II) cations was evaluated spectrophotometrically at different reaction conditions (pH, reaction time, metal-to-ligand molar ratio). The results showed that immediately after mixing the reagents, pH 7.4, complex species of composition PdHL existed predominantly with a value of conditional stability constant lgβ'=6.52. The reaction was completed within 24 hours affording the formation of species Pd2L with significantly increased stability (lgβ'=9.34). The spectral data suggest that obidoxime coordinates metal(II) ions through the oximate functional groups. The in vitro reactivation assay of paraoxon-inhibited rat brain acetylcholinesterase revealed that the new complex species were much less active than the non-coordinated obidoxime. The lack of reactivation ability could be explained by the considerable stability of complexes in solution as well as by the deprotonation of oxime groups essential for recovery of the enzymatic activity.
