Molecular interaction of 2-mercaptobenzimidazole with catalase reveals a potentially toxic mechanism of the inhibitor
Molecular interaction of 2-mercaptobenzimidazole with catalase reveals a potentially toxic mechanism of the inhibitor
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2-巯基苯并咪唑与过氧化氢酶的分子相互作用揭示了该抑制剂的潜在毒性机制
DOI：
10.1016/j.jphotobiol.2014.09.018
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发表时间：
2014-12-01
影响因子：
5.4
通讯作者：
Zong, Wansong
中科院分区：
文献类型：
--
作者：
Teng, Yue;Zou, Luyi;Zong, Wansong
2-巯基苯并咪唑（MBI）作为缓蚀剂、镀铜光亮剂和橡胶促进剂被广泛应用。MBI在环境中的残留对人体健康具有潜在的风险。本工作采用光谱和分子对接的方法，在生理条件下研究了MBI与重要的抗氧化酶过氧化氢酶（CAT）的毒性相互作用。MBI可通过氢键和货车范德华力与CAT单位点结合形成MBI-CAT复合物。分子对接研究表明，MBI结合到CAT链B和C的CAT界面，导致CAT构象和微环境发生变化，进而抑制CAT活性。本研究在分子水平上提供了直接证据，表明暴露于MBI可诱导酶CAT的结构和功能发生变化。（C）2014 Elsevier B. V.保留所有权利。
2-Mercaptobenzimidazole (MBI) is widely utilized as a corrosion inhibitor, copper-plating brightener and rubber accelerator. The residue of MBI in the environment possesses a potential risk to human health. In this work, the toxic interaction of MBI with the important antioxidant enzyme catalase (CAT) was investigated using spectroscopic and molecular docking methods under physiological conditions. MBI can spontaneously bind with CAT with one binding site through hydrogen bonds and van der Waals forces to form MBI-CAT complex. The molecular docking study revealed that MBI bound into the CAT interface of chains B and C, which led to some conformational and microenvironmental changes of CAT and further resulted in the inhibition of CAT activity. This present study provides direct evidence at a molecular level to show that exposure to MBI could induce changes in the structure and function of the enzyme CAT. (C) 2014 Elsevier B.V. All rights reserved.