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The benzene metabolite p-benzoquinone inhibits the catalytic activity of bovine liver catalase: A biophysical study. | LitMetric

The benzene metabolite p-benzoquinone inhibits the catalytic activity of bovine liver catalase: A biophysical study.

Int J Biol Macromol

Centre of Excellence in Integrated Omics & Computational Biology, Utkal University, Bhubaneswar 751004, Odisha, India; Post Graduate Department of Biotechnology, Utkal University, Bhubaneswar 751004, Odisha, India. Electronic address:

Published: January 2021

AI Article Synopsis

  • The study investigates how para-benzoquinone (p-BQ) affects the structure and function of bovine liver catalase (BLC), an important antioxidant enzyme, highlighting that p-BQ inhibits BLC activity.
  • It finds that the binding strength between p-BQ and BLC varies significantly depending on the buffer used, being strongest in Tris buffer and weak in HEPES buffer, and is influenced by hydrogen bonding and van der Waals interactions.
  • Findings suggest that p-BQ induces conformational changes in BLC, which lead to reduced enzyme activity and altered properties, demonstrated by changes in absorbance and fluorescence as the p-BQ concentration increases.

Article Abstract

The current communication reports the inhibitory effect of para-benzoquinone (p-BQ) on the structure and function of bovine liver catalase (BLC), a vital antioxidant enzyme. Both BLC and p-BQ were dissolved in respective buffers and the biophysical interaction was studied at physiological concentrations. For the first time our data reveals an enthalpy-driven interaction between BLC and p-BQ which is due to hydrogen bonding and van der Waals interactions. The binding affinity of p-BQ with BLC is nearly 2.5 folds stronger in MOPS buffer than Phosphate buffer. Importantly, the binding affinity between BLC and p-BQ was weak in HEPES buffer as compared to other buffers being the strongest in Tris buffer. Molecular docking studies reveal that binding affinity of p-BQ with BLC differ depending upon the nature of buffers rather than on the participating amino acid residues of BLC. This is further supported by the differential changes in secondary structures of BLC. The p-BQ-induced conformational change in BLC was evident from the reduced BLC activity in presence of different buffers in the following order, Phosphate>MOPS>Tris>HEPES. The absorbance peak of BLC was gradually increased and fluorescence spectra of BLC were drastically decreased when BLC to p-BQ molar ratio was incrementally enhanced from 0 to 10,000 times in presence of all buffers. Nevertheless, the declined activity of BLC was positively correlated with the reduced fluorescence and negatively correlated with the enhanced absorbance. Electrochemical study with cyclic voltammeter also suggests a direct binding of p-BQ with BLC in presence of different buffers. Thus, p-BQ-mediated altered secondary structure in BLC results into compromised activity of BLC.

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Source
http://dx.doi.org/10.1016/j.ijbiomac.2020.11.044DOI Listing

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