标题:Potential enzyme toxicity of oxytetracycline to catalase
作者:Chi, Z.;Liu, R.;Zhang, H.
作者机构:[Chi, Z] School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment and Health, Shandong Province, 27# Sh 更多
通讯作者:Liu, R
通讯作者地址:[Liu, RT]Shandong Univ, Sch Environm Sci & Engn, China Amer CRC Environm & Hlth, 27 Shanda South Rd, Jinan 250100, Shandong, Peoples R China.
来源:Science of the Total Environment
出版年:2010
卷:408
期:22
页码:5399-5404
DOI:10.1016/j.scitotenv.2010.08.005
关键词:Catalase;Enzyme toxicity;Non-covalent binding;Oxytetracycline;Spectroscopic techniques
摘要:Oxytetracycline (OTC) is a kind of widely used veterinary drugs. The residue of OTC in the environment is potentially harmful. In the present work, the non-covalent toxic interaction of OTC with catalase was investigated by the fluorescence spectroscopy, UV-vis absorption and circular dichroism (CD) spectroscopy at physiological pH 7.4. OTC can interact with catalase to form a complex mainly by van der Waals\' interactions and hydrogen bonds with one binding site. The association constants K were determined to be K_(293K)=7.09×10~4Lmol~(-1) and K_(311K)=3.31×10~4Lmol~(-1). The thermodynamic parameters (ΔH°, ΔG° and ΔS°) of the interaction were calculated. Based on the F?rster theory of non-radiative energy transfer, the distance between bound OTC and the tryptophan residues of catalase was determined to be 6.48nm. The binding of OTC can result in change of the micro-environment of the tryptophan residues and the secondary structure of catalase. The activity of catalase was also inhibited for the bound OTC. This work establishes a new strategy to probe the enzyme toxicity of veterinary drug residues and is helpful for clarifying the molecular toxic mechanism of OTC in vivo. The established strategy can be used to investigate the potential enzyme toxicity of other small organic pollutants and drugs.
收录类别:EI;SCOPUS;SCIE
WOS核心被引频次:26
Scopus被引频次:26
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-77956880315&doi=10.1016%2fj.scitotenv.2010.08.005&partnerID=40&md5=ac789cc983a55771b18e1a2eb59731c3
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