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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
Direct electrochemistry and electrocatalysis of hemoglobin at mesoporous carbon modified electrode
Supeng Pei1, Song Qu, Yongming Zhang
1School of Chemistry and Chemical Engineering, Shanghai Jiao Tong University, Shanghai 200240, China. peisupeng@sjtu.edu.cn
Abstract:
The novel highly ordered mesoporous carbon (known as FDU-15), prepared by the organic-organic self-assembly method was been used for first time for the immobilization of hemoglobin (Hb) and its bioelectrochemical properties were studied. The resulting Hb/FDU-15 film provided a favorable microenvironment for Hb to perform direct electron transfers at the electrode. The immobilized Hb also displayed its good electrocatalytic activity for the reduction of hydrogen peroxide. The results demonstrate that mesoporous carbon FDU-15 can improve the Hb loading with retention of its bioactivity and greatly promote the direct electron transfer, which can be attributed to its high specific surface area, uniform ordered porous structure, suitable pore size and biocompatibility. Our present study may provide an alternative way for the construction of nanostructure biofunctional surfaces and pave the way for its application to biosensors.
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