Understanding Ligninase-Mediated Reactions of Endocrine Disrupting Chemicals in Water: Reaction Rates and Quantitative Structure鈥揂ctivity Relationships

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• 作者：Liang Mao ; Lisa M. Colosi ; Shixiang Gao ; Qingguo Huang
• 刊名：Environmental Science & Technology
• 出版年：2011
• 出版时间：July 15, 2011
• 年：2011
• 卷：45
• 期：14
• 页码：5966-5972
• 全文大小：875K
• 年卷期：v.45,no.14(July 15, 2011)
• ISSN：1520-5851

文摘

We have verified in our previous work that lignin peroxidase (LiP) mediates effective removal of selected natural and synthetic estrogens. The efficiency of these reactions was greatly enhanced in the presence of veratryl alcohol (VA), a chemical that is produced along with LiP by certain white rot fungi, for example, Phanerochaete chrysosporium. In this study, we systematically evaluated the kinetic behaviors of LiP-mediated reactions for six endocrine disrupting compounds (EDCs), that is, steroid estrogens and their structural analogs, in both the presence and absence of VA. Resulting kinetic parameters were then correlated with structural features of LiP/substrate binding complexes, as quantified using molecular simulation, to create quantitative structure鈥揳ctivity relationship (QSAR) equations. These equations suggest that binding distance between a substrate鈥檚 phenolic proton and 未N of HIS47鈥瞫 imidazole ring plays an important role in modulating substrate reactivity toward LiP in both the presence and absence of VA. This information provides insight into an important enzymatic reaction process that occurs in the natural environment affecting EDC transformation, a process that may be used in engineered systems to achieve EDC removal from water.