4.8 Article

Bismuth Oxyiodide Couples with Glucose Oxidase: A Special Synergized Dual-Catalysis Mechanism for Photoelectrochemical Enzymatic Bioanalysis

期刊

ACS APPLIED MATERIALS & INTERFACES
卷 10, 期 4, 页码 3372-3379

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acsami.7b17647

关键词

photoelectrochemical bioanalysis; cathodic; BiOI; glucose oxidases; H2O2

资金

  1. National Natural Science Foundation of China [21327902, 21675080]
  2. Natural Science Foundation of Jiangsu Province [BK20161484, BK20170073]
  3. Fundamental Research Funds for the Central Universities [NE2015003]
  4. Six Talent Peaks Program of Jiangsu Province [2013-XNY-010]
  5. Scientific Research Foundation of Graduate School of Nanjing University [2016CL06]
  6. Priority Academic Program Development of Jiangsu Higher Education Institutions

向作者/读者索取更多资源

On the basis of a special synergized dual-catalysis mechanism, this work reports the preparation of a BiOI-based heterojunction and its use for cathodic photoelectrochemical (PEC) oxidase biosensing, which, unexpectedly, revealed that hydrogen peroxide (H2O2) had a greater impact than dioxygen (O-2). Specifically, the BiOI layer was in situ formed on the substrate through an impregnating hydroxylation method for the following coupling with the model enzyme of glucose oxidases (GOx). The constructed cathodic PEC enzyme sensor exhibited a good analytical performance of rapid response, high stability, and good selectivity. Especially, glucose-induced H2O2-controlled enhancement of the photocurrent was recorded rather than the commonly observed O-2-dependent suppression of the signal. This interesting phenomenon was attributed to a special synergized dual-catalysis mechanism. Briefly, this study is expected to provide a new BiOI-based photocathode for general PEC bioanalysis development and to inspire more interest in the design and construction of a novel heterojunction for advanced photocathodic bioanalysis. More importantly, the mechanism revealed here would offer a totally different perspective for the use of a biomimetic catalyst in the design of future PEC enzymatic sensing and the understanding of relevant signaling routes as well as the implementation of innovative PEC devices.

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