Molecular interaction mechanism between 2-mercaptobenzimidazole and copper-zinc superoxide dismutase.

Clicks: 232
ID: 98885
2014
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Abstract
2-Mercaptobenzimidazole (MBI) is widely utilized as a corrosion inhibitor, copper-plating brightener and rubber accelerator. The residue of MBI in the environment is potentially harmful. In the present work, the toxic interaction of MBI with the important antioxidant enzyme copper-zinc superoxide dismutase (Cu/ZnSOD) was investigated using spectroscopic and molecular docking methods. MBI can interact with Cu/ZnSOD to form an MBI-Cu/ZnSOD complex. The binding constant, number of binding sites and thermodynamic parameters were measured, which indicated that MBI could spontaneously bind with Cu/ZnSOD with one binding site through hydrogen bonds and van der Waals forces. MBI bound into the Cu/ZnSOD interface of two subdomains, which caused some microenvironmental and secondary structure changes of Cu/ZnSOD and further resulted in the inhibition of Cu/ZnSOD activity. This work provides direct evidence at a molecular level to show that exposure to MBI could induce changes in the structure and function of the enzyme Cu/ZnSOD. The estimated methods in this work may be applied to probe molecular interactions of biomacromolecules and other pollutants and drugs.
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teng2014molecularplos Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Teng, Yue;Zou, Luyi;Huang, Ming;Chen, Yadong;
Journal PloS one
Year 2014
DOI
DOI not found
URL
http://europepmc.org/articles/PMC4144957?pdf=render
Keywords
chemistry Organic Chemistry Medicine Science

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