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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 myoglobin-based nanocomposite membrane electrode
Yancai Li1, Yuanjun Li, Yiyun Yang
1Chemistry Department of Zhangzhou Normal University, N36 Zhangzhou, Zhangzhou, 363000, PR China. liyancai2000@yahoo.com.cn
Abstract:
The direct electron transfer of myoglobin (Mb) was achieved based on the immobilization of Mb/Silver nanoparticles (AgNPs) on glassy carbon electrode by multi-wall carbon nanotubes (MWNTs)-chitosan(Chit) film. The immobilized Mb displayed a pair of well-defined and reversible redox peaks with a formal potential (E(θ')) of -24 mV (vs. Ag/AgCl) in 0.1 M pH 7.0 phosphate buffer solution. The apparent heterogeneous electron transfer rate constants (k(s)) of Mb confined to Chit-MWNTs film was evaluated as 5.47 s(-1) according to Laviron's equation. The surface concentration (Γ(*)) of the electroactive Mb in the Chit-MWNTs film was estimated to be (4.16±0.35)×10(-9) mol cm(-2). Meanwhile, the catalytic ability of Mb toward the reduction of H(2)O(2) was studied. Its apparent Michaelis-Menten constant for H(2)O(2) was 0.024 mM, showing a good affinity. The linear range for H(2)O(2) determination was from 2.5×10(-5) M to 2.0×10(-4) M with a detection limit of 1.02×10(-6) M (S/N=3). Moreover, the biosensor displays rapid response to H(2)O(2) and good stability and reproducibility.
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