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Exploring the functional changes and binding mechanism of bovine liver catalase in the presence of Schiff base complexes. Comprehensive spectroscopic studies

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Abstract

Nowadays, efforts to synthesize new compounds with medicinal activity, including antioxidant properties, have increased because they are delay, prevent, or removes oxidative damage to target cells. The interaction of these compounds with biological molecules like catalase (as an important antioxidant enzyme) is very important in the process of improving the properties of them. So, in this research two mixed-ligand complexes with divalent ion Zn containing novel Schiff base ligand of 4-pyridylimine-1,2-diacetylmonoxime as a primary ligand and 2,2-Bipyridine (bpy, in complex a) and 1,10-phenanthroline (phen, in complex b) as secondary ligands were synthesized and successfully characterized using various spectrochemical techniques. The antioxidant capacity of the synthesized complexes was studied in vitro by 2,2-diphenyl-1-picrylhydrazyl free radical scavenging method. Results revealed that the synthesized complexes presented moderate antioxidant activity compared to vitamin C (IC50(Complex a) = 0.55 mol L−1, IC50(Complex b) = 0.63 mol L−1, IC50(Vit C) = 0.045 mol L−1). Biophysical techniques were used to study the binding of these complexes with bovine liver catalase (BLC), as an antioxidant model protein. The trial findings showed the interaction between Schiff base complexes and BLC with a relatively strong binding affinity (Kb = 2.0 × 105 M−1 for complex a and 0.73 × 105 M−1 for complex b at 310 K). An intense fluorescence quenching of enzyme through a static quenching mechanism was occurred due to the binding of both complexes to BLC. Hydrogen bonds and van der Waals forces in both examined systems were the main stabilizing forces in the development of drug-protein complex. The secondary structure of BLC was changed in the presence of Zn complexes; decreased α-helix and increased β-sheet contents confirmed the protein instability during the interaction. Considering that the most important structural difference between a and b is in their secondary ligands, it can be concluded that the presence phen ligand compared to bpy leads to more interactions as well as more changes in enzyme activity.

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Acknowledgements

This work was funded by University of Zabol (Grant No. UOZGR-9618-2).

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Authors and Affiliations

  1. Department of Chemistry, Faculty of Science, University of Sistan and Baluchestan, Zahedan, Iran

    Hadi Nouri & Hassan Mansouri-Torshizi

  2. Department of Chemistry, Faculty of Science, University of Zabol, Zabol, Iran

    Somaye Shahraki

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  1. Hadi Nouri
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Correspondence to Hassan Mansouri-Torshizi or Somaye Shahraki.

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Nouri, H., Mansouri-Torshizi, H. & Shahraki, S. Exploring the functional changes and binding mechanism of bovine liver catalase in the presence of Schiff base complexes. Comprehensive spectroscopic studies. J IRAN CHEM SOC 18, 3281–3294 (2021). https://doi.org/10.1007/s13738-021-02266-0

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