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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 immobilized in TiO2 nanotube films
1LTCS and Department of Advanced Materials and Nanotechnology, College of Engineering, Peking University, Beijing 100871, China.
Abstract:
Titanium oxide nanotubes (TiO(2)-NTs) synthesized by the hydrothermal method had been prepared as the co-immobilization matrix to incorporate hemoglobin (Hb) successfully. The nanostructures of TiO(2)-NTs were investigated by X-ray diffraction and high-resolution electron microscopy. The Hb immobilized in TiO(2)-NTs had a similar structure to the native of Hb and retained its near-native conformations as characterized by the UV-vis and FT-IR spectroscopy. A couple of quasi-reversible redox peaks with a formal potential of -0.34 V (vs. SCE) in 0.10 M pH 7.0 phosphate buffered saline (PBS) were observed. The amperometric response of the immobilized Hb linearly to H(2)O(2) concentration ranged from 4 microM to 64 microM with a detection limit of 4.637 x 10(-6)M and the high stability of the immobilized Hb in TiO(2)-NTs constituted a promising platform for the development of biosensors.
