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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
A hydrogen peroxide biosensor based on the direct electron transfer of hemoglobin encapsulated in liquid-crystalline
Feng Gao1, Zhen Yao, Qin'an Huang
1Anhui Key Laboratory of Chemo/Biosensing, Anhui Key Laboratory of Functional Molecular Solids, College of Chemistry and Materials Science, Anhui Normal University, Wuhu 241000, China. fgao@mail.ahnu.edu.cn
Abstract:
Liquid crystal cubic phase formed with monoolein has been used as immobilizing matrix to host redox protein hemoglobin on glassy carbon electrode surface. The promoted direct electron transfer between hemoglobin and electrode was observed and a large average kinetic electron transfer rate constant k(s) of 3.03(±0.02)s(-1) was estimated. The electrode modified with cubic phase containing hemoglobin retains the bioactivity of hemoglobin and shows excellent bioelectrocatalytic activity to the reduction of hydrogen peroxide with a small apparent Michaelis-Menten constant of 0.25(±0.03)mM. A novel reagentless hydrogen peroxide biosensor was constructed using the hemoglobin-containing cubic phase modified electrode and the proposed hydrogen peroxide biosensor shows a linear range of 7.0-239μM with a detection limit of 3.1(±0.2)μM and good stability and reproducibility.
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