| 铜离子配位甲烷氧化菌素功能化纳米金模拟过氧化物酶的研究 |
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| 引用本文： | 李春雨,辛嘉英,林惠颖,张悦,夏春谷.铜离子配位甲烷氧化菌素功能化纳米金模拟过氧化物酶的研究[J].分子催化,2017,31(5):480-485. |
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| 作者姓名： | 李春雨 辛嘉英 林惠颖 张悦 夏春谷 |
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| 作者单位： | 1. 哈尔滨商业大学食品科学与工程重点实验室,黑龙江哈尔滨,150076;2. 哈尔滨商业大学食品科学与工程重点实验室,黑龙江哈尔滨150076;中国科学院兰州化学物理研究所羰基合成与选择氧化国家重点实验室,甘肃兰州730000;3. 中国科学院兰州化学物理研究所羰基合成与选择氧化国家重点实验室,甘肃兰州,730000 |
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| 基金项目： | 国家自然科学基金项目（21073050，21573055）；北京化工大学资源有效利用国家重点实验室开放课题（CRE-2015-C-104）和哈尔滨商业大学创新团队项目资助（2016TD006） |
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| 摘 要： | 合成了纳米金-甲烷氧化菌素(Mb)-铜配合物,该配合物可以作为模拟过氧化物酶用于催化过氧化氢氧化对苯二酚的反应.通过紫外光谱、荧光光谱、红外光谱对纳米金-甲烷氧化菌素(Mb)-铜进行了表征.利用紫外-可见分光光度法研究了配合物催化过氧化氢氧化对苯二酚的动力学.考察了体系p H、体系温度及过氧化氢/催化剂摩尔比对催化反应速率的影响.结果表明纳米金-甲烷氧化菌素(Mb)-铜配合物符合生物催化剂条件影响的一般规律,但比生物酶具有更高的热稳定性.
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| 关 键 词： | 甲烷氧化菌素 纳米金 模拟过氧化物酶 |
| 收稿时间： | 2017/7/3 0:00:00 |
| 修稿时间： | 2017/8/10 0:00:00 |
Study on Functionalized Gold Nanoparticles of Methanobactin by Copper Ion Coordination Uesd as Simulated Peroxidase |
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| LI Chun-yu,XIN Jia-ying,LIN Hui-ying,ZHANG Yue and XIA Chun-gu.Study on Functionalized Gold Nanoparticles of Methanobactin by Copper Ion Coordination Uesd as Simulated Peroxidase[J].Journal of Molecular Catalysis (China),2017,31(5):480-485. |
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| Authors: | LI Chun-yu XIN Jia-ying LIN Hui-ying ZHANG Yue and XIA Chun-gu |
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| Institution: | Key Laboratory for Food Science and Engineering, Harbin University of Commerce, Harbin 150076, China,Key Laboratory for Food Science and Engineering, Harbin University of Commerce, Harbin 150076, China;State Key Laboratory for Oxo Synthesis and Selective Oxidation, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, China,Key Laboratory for Food Science and Engineering, Harbin University of Commerce, Harbin 150076, China,Key Laboratory for Food Science and Engineering, Harbin University of Commerce, Harbin 150076, China and State Key Laboratory for Oxo Synthesis and Selective Oxidation, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, China |
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| Abstract: | In this paper, AuNPs-methanobactin(Mb)-copper complexes have been synthesized, which can be used as a simulated peroxidase in the catalytic oxidation of hydroquinone by H2O2. AuNPs-methanobactin(Mb)-copper was characterized by UV spectroscopy, fluorescence spectroscopy and infrared spectroscopy. The kinetics of hydroquinone oxidation catalyzed by complexes were studied by UV-Vis spectrophotometry. The effects of system pH, system temperature and hydroquinone/complex molar ratio on the catalytic reaction rate were investigated. The results showed that the AuNPs-methanobactin(Mb)-copper complex conformed to the general rule of the influence of the biocatalyst condition, but having higher thermal stability than the biological enzyme. |
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| Keywords: | methanobactin gold nanoparticles simulated peroxidase |
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