Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery
Apstrakt
The aim of this work was to investigate the influence of [PdCl4](2-), [PdCl(dien)](+) and [PdCl(Me(4)dien)](+) complexes on Na+/K+-ATPase activity. The dose-dependent inhibition curves were obtained in all cases. IC50 values determined by Hill analysis were 2.25 x 10(-5) M, 1.21 x 10(-4) Mand 2.36 x 10(-4) M, respectively. Na+/K+-ATPase exhibited typical Michelis-Menten kinetics in the presence of Pd(II) complexes. Kinetic parameters (V-max, K-m) derived using Eadie - Hofstee transformation indicated a noncompetitive type of Na+/K+-ATPase inhibition. The inhibitor constants (K-i) were determined from Dixon plots. The order of complex affinity for binding with Na+/K+-ATPase, deducted from K-i values, was [PdCl4](2-) GT [PdCl(dien)]+ GT [ PdCl(Me(4)dien)](+). The results indicated that the potency of Pd(II) complexes to inhibit Na+/K+-ATPase activity depended strongly on ligands of the related compound. Furthermore, the ability of SH-donor ligands, L-cysteine and glutathione, to prevent ...and recover the Pd(II) complexes-induced inhibition of Na+/K+-ATPase was examined. The addition of 1mM L-cysteine or glutathione to the reaction mixture before exposure to Pd(II) complexes prevented the inhibition by increasing the IC50 values by one order of magnitude. Moreover, the inhibited enzymatic activity was recovered by addition of SH-donor ligands in a concentration-dependent manner.
Ključne reči:
Na+/K+-ATPase / Pd(II) complexes / inhibition / kinetics / prevention and recoveryIzvor:
Journal of Enzyme Inhibition and Medicinal Chemistry, 2006, 21, 4, 459-465
DOI: 10.1080/14756360600628510
ISSN: 1475-6366
PubMed: 17059181
WoS: 000240322000017
Scopus: 2-s2.0-33748527199
Kolekcije
Institucija/grupa
VinčaTY - JOUR AU - Krinulović, Katarina AU - Vasić, Vesna M. PY - 2006 UR - https://vinar.vin.bg.ac.rs/handle/123456789/3080 AB - The aim of this work was to investigate the influence of [PdCl4](2-), [PdCl(dien)](+) and [PdCl(Me(4)dien)](+) complexes on Na+/K+-ATPase activity. The dose-dependent inhibition curves were obtained in all cases. IC50 values determined by Hill analysis were 2.25 x 10(-5) M, 1.21 x 10(-4) Mand 2.36 x 10(-4) M, respectively. Na+/K+-ATPase exhibited typical Michelis-Menten kinetics in the presence of Pd(II) complexes. Kinetic parameters (V-max, K-m) derived using Eadie - Hofstee transformation indicated a noncompetitive type of Na+/K+-ATPase inhibition. The inhibitor constants (K-i) were determined from Dixon plots. The order of complex affinity for binding with Na+/K+-ATPase, deducted from K-i values, was [PdCl4](2-) GT [PdCl(dien)]+ GT [ PdCl(Me(4)dien)](+). The results indicated that the potency of Pd(II) complexes to inhibit Na+/K+-ATPase activity depended strongly on ligands of the related compound. Furthermore, the ability of SH-donor ligands, L-cysteine and glutathione, to prevent and recover the Pd(II) complexes-induced inhibition of Na+/K+-ATPase was examined. The addition of 1mM L-cysteine or glutathione to the reaction mixture before exposure to Pd(II) complexes prevented the inhibition by increasing the IC50 values by one order of magnitude. Moreover, the inhibited enzymatic activity was recovered by addition of SH-donor ligands in a concentration-dependent manner. T2 - Journal of Enzyme Inhibition and Medicinal Chemistry T1 - Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery VL - 21 IS - 4 SP - 459 EP - 465 DO - 10.1080/14756360600628510 ER -
@article{ author = "Krinulović, Katarina and Vasić, Vesna M.", year = "2006", abstract = "The aim of this work was to investigate the influence of [PdCl4](2-), [PdCl(dien)](+) and [PdCl(Me(4)dien)](+) complexes on Na+/K+-ATPase activity. The dose-dependent inhibition curves were obtained in all cases. IC50 values determined by Hill analysis were 2.25 x 10(-5) M, 1.21 x 10(-4) Mand 2.36 x 10(-4) M, respectively. Na+/K+-ATPase exhibited typical Michelis-Menten kinetics in the presence of Pd(II) complexes. Kinetic parameters (V-max, K-m) derived using Eadie - Hofstee transformation indicated a noncompetitive type of Na+/K+-ATPase inhibition. The inhibitor constants (K-i) were determined from Dixon plots. The order of complex affinity for binding with Na+/K+-ATPase, deducted from K-i values, was [PdCl4](2-) GT [PdCl(dien)]+ GT [ PdCl(Me(4)dien)](+). The results indicated that the potency of Pd(II) complexes to inhibit Na+/K+-ATPase activity depended strongly on ligands of the related compound. Furthermore, the ability of SH-donor ligands, L-cysteine and glutathione, to prevent and recover the Pd(II) complexes-induced inhibition of Na+/K+-ATPase was examined. The addition of 1mM L-cysteine or glutathione to the reaction mixture before exposure to Pd(II) complexes prevented the inhibition by increasing the IC50 values by one order of magnitude. Moreover, the inhibited enzymatic activity was recovered by addition of SH-donor ligands in a concentration-dependent manner.", journal = "Journal of Enzyme Inhibition and Medicinal Chemistry", title = "Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery", volume = "21", number = "4", pages = "459-465", doi = "10.1080/14756360600628510" }
Krinulović, K.,& Vasić, V. M.. (2006). Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery. in Journal of Enzyme Inhibition and Medicinal Chemistry, 21(4), 459-465. https://doi.org/10.1080/14756360600628510
Krinulović K, Vasić VM. Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2006;21(4):459-465. doi:10.1080/14756360600628510 .
Krinulović, Katarina, Vasić, Vesna M., "Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery" in Journal of Enzyme Inhibition and Medicinal Chemistry, 21, no. 4 (2006):459-465, https://doi.org/10.1080/14756360600628510 . .