Construction of a Novel Guest Biomimetic Glutathione Peroxidase With Solvent-Dependent Catalytic Behavior by Incorporating the Active Center Into Adamantyl Molecule
Yanzhen Yinab, Chao Langc, Xiaoxi Hua, Zhongfeng Shia, Yun Wanga, Shufei Jiaoa, #, Chengxiang Caia, Junqiu Liuc
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a School of Chemistry and Chemical Engineering, Qinzhou University, No.89, Xihuan Nanlu, Qinzhou 535000, People’s Republic of China; b Guangxi Experiment Centre of Science and Technology, Guangxi University, Nanning 530004, China; c State Key Laboratory of Supramolecular Structure and Materials, Jilin University, Changchun 130012, People’s Republic of China
Received May 22, 2013; in final form August 1, 2013
A novel guest biomimetic glutathione peroxidase(3,3'-tellurobis(propane-3,1-diyl) diadamantanecarboxylate, denoted as ADA-Te-ADA) was synthesized. ADA-Te-ADA functioned to overcome the disadvantages in the construction of building block for giant supramolecular biomimetic enzyme. To reveal the catalytic property of hydrophobic ADA-Te-ADA, the catalytic mechanism was investigated using PBS (phosphate buffer (pH=7.0. 50mM))/methanol solvent mixture as assay solution. It indicated that ADA-Te-ADA exhibited typical enzyme catalytic behavior by saturation kinetics measurement. Importantly, ADA-Te-ADA exhibited the typical solvent-dependent catalytic behavior. And the highest catalytic rate 4.29 μM.min–1 was obtained when the volume ratio of PBS:methanol was 5:5. Especially, the catalytic rates obtained based on various substrates proved that ADA-Te-ADA slightly displayed special substrate selectivity, which was the ideal catalytic characterization of building block for giant supramolecular biomimetic enzyme. The successfully synthesis of ADA-Te-ADA might highlight for the understanding of the catalytic mechanism of hydrophobic guest biomimetic glutathione peroxidase. And it also might provide the basement for the construction of giant supramolecular biomimetic enzyme.
Keywords: Biomimetic enzymes, Biocatalysis, Biomimetics, Enzyme activity, Glutathione peroxidase.
Áèîîðã. õèìèÿ 2014, 40 (2): 178-185