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

Title Bismuth Oxyiodide Couples with Glucose Oxidase: A Special Synergized Dual-catalysis Mechanism for Photoelectrochemical Enzymatic Bioanalysis.
Authors L. Zhang; Y.F. Ruan; Y.Yu Liang; W.W. Zhao; X.D. Yu; J.J. Xu; H.Y. Chen
Journal ACS Appl Mater Interfaces
DOI 10.1021/acsami.7b17647
Abstract

On the basis of a special synergized dual-catalysis mechanism, this work reports the preparation of BiOI-based heterojunction and its use for cathodic photoelectrochemical (PEC) oxidase biosensing, which, unexpectedly, revealed that H2O2 impacted greater than O2. Specifically, 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 good analytical performance of rapid response, high stability, and good selectivity. Especially, the glucose-induced H2O2-controlled enhancement of the photocurrent was recorded, rather than the commonly observed O2-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 interests in the design and construction of novel heterojunction for advanced photocathodic bioanalysis. More importantly, the mechanism revealed here would offer a totally different perspective for the use of 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.

Citation L. Zhang; Y.F. Ruan; Y.Yu Liang; W.W. Zhao; X.D. Yu; J.J. Xu; H.Y. Chen.Bismuth Oxyiodide Couples with Glucose Oxidase: A Special Synergized Dual-catalysis Mechanism for Photoelectrochemical Enzymatic Bioanalysis.. ACS Appl Mater Interfaces. 2018. doi:10.1021/acsami.7b17647

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