Modulation of antioxidant enzyme by light and heavy rare earth metals: A case study with catalase

被引:0
作者
Samal, Rashmi R. [1 ,2 ]
Subudhi, Umakanta [1 ,2 ]
机构
[1] Biochemistry & Biophysics Laboratory, Environment & Sustainability Department, CSIR-Institute of Minerals & Materials Technology, Bhubaneswar
[2] Academy of Scientific and Innovative Research (AcSIR), Ghaziabad
关键词
Catalase; Enzyme kinetics; Gadolinium; Lanthanides; Metal; Praseodymium; Rare earth elements;
D O I
10.1016/j.ijbiomac.2024.137820
中图分类号
学科分类号
摘要
The present study highlights the hazardous effect of heavy and light rare earth elements (REEs) on bovine liver catalase (BLC) using a combination of spectroscopic and computational methods. The presence of Praseodymium chloride (PrCl3) and Gadolinium chloride (GdCl3) resulted in a substantial reduction in catalytic efficiency of BLC by approximately 1.8 and 2.6 fold, respectively. The compromised activity was further accompanied by conformational rearrangements at the secondary and tertiary levels as evidenced by circular dichroism (CD) and fluorescence spectroscopy. These analyses revealed a significant decrease in α-helical content and a simultaneous increase in random coils, disrupting intramolecular hydrogen bonding. Furthermore, the zeta potential (ζ) of BLC demonstrated a reversal from negative to positive ζ values upon the addition of PrCl3 and GdCl3, indicating BLC-lanthanide complex formation. Isothermal titration calorimetry (ITC) supports spontaneous interaction with negative free energy favouring endothermic reaction. This was further supported by docking studies which revealed the binding of PrCl3 and GdCl3 within the active site of BLC thus interfering with the catalytic ability to degrade hydrogen peroxide (H2O2). Nevertheless, a significant decline in the melting temperature (Tm) of BLC was observed in the presence of lanthanides suggesting the thermal instability of the enzyme. Thus, a similar approach could be applied to evaluate the hazardous effects of lanthanides on structural and functional changes in other proteins or similar biomolecules. © 2024 Elsevier B.V.
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