Selenium-Mediated Micellar Catalyst: An Efficient Enzyme Model for Glutathione Peroxidase-like Catalysis

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• 作者：Xin Huang ; Zeyuan Dong ; Junqiu Liu ; Shizhong Mao ; Jiayun Xu ; Guimin Luo ; Jiacong Shen
• 刊名：Langmuir
• 出版年：2007
• 出版时间：January 30, 2007
• 年：2007
• 卷：23
• 期：3
• 页码：1518 - 1522
• 全文大小：74K
• 年卷期：v.23,no.3(January 30, 2007)
• ISSN：1520-5827

文摘

Mimicking the properties of the selenoenzyme glutathione peroxidase (GPx) has inspired great interest. In thisreport, a selenium-containing micellar catalyst was successfully constructed by the self-assembly of the cationicsurfactant hexadecyltrimethylammonium bromide (CTAB) with benzeneseleninic acid (PhSeO₂H) through hydrophobicand electrostatic interaction in water. The selenium-containing micellar catalyst demonstrated substrate specificity forboth 3-carboxy-4-nitrobenzenethiol (ArSH, 2) and cumene hydroperoxide (CUOOH), and their complexation wasconfirmed by UV and fluorescence spectra. More importantly, it demonstrated high GPx activity in two assay systems.It is about 126 times more effective than the well-known GPx mimic ebselen in the classical coupled reductase assaysystem; however, by using hydrophobic substrate ArSH (2) as an alternative of glutathione (GSH, 1), the micellarcatalyst exhibited remarkable 500-fold and 94 500-fold rate enhancements compared with that of PhSeO₂H andPhSeSePh.