Molecular Hydrogel-Stabilized Enzyme with Facilitated Electron Transfer for Determination of H2O2 Released from Live Cells

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• 作者：Jie Zhou ; Chuanan Liao ; Limin Zhang ; Qigang Wang ; Yang Tian
• 刊名：Analytical Chemistry
• 出版年：2014
• 出版时间：May 6, 2014
• 年：2014
• 卷：86
• 期：9
• 页码：4395-4401
• 全文大小：397K
• 年卷期：v.86,no.9(May 6, 2014)
• ISSN：1520-6882

文摘

In this work, small molecular hydrogel was first employed as a surrounding matrix to stabilize an enzyme model, Cytochrome c (Cyt c), and more importantly to facilitate electron transfer between redox enzyme and electrode. Direct electron transfer of Cyt c was successfully achieved in the molecular hydrogel with redox formal potential (E^{0鈥?/sup>) of 100.7 卤 3.2 mV versus Ag|AgCl and heterogeneous electron transfer rate constant (k_s) up to 18.6 卤 2.3 s鈥?. Experimental data demonstrated that Cyt c was stably immobilized into the molecular hydrogel and retained its inherent bioactive activity toward H₂O₂. The direct redox reaction of Cyt c, followed by the biochemical reaction between Cyt c and H₂O₂, established a reliable approach to determine H₂O₂ at an optimized potential with high selectivity over other reactive oxygen species (ROS), oxygen, metal ions, ascobic acid (AA), and so on. In addition, the present biosensor for H₂O₂ also exhibited wide linear range and low detection limit, which fulfills the requirements for detection of H₂O₂ in a biological system. The remarkable analytical performance of the present biosensor, as well as the long-term stability and good reproducibility ascribed to the molecular hydrogel-stabilized enzyme, provided a durable platform for real-time determination of H₂O₂ from live cells.}