Investigation on electrochemical behavior and its catalytic effect on oxygen reduction reaction of 3-Ferrocenyl dihydropyrazole derivative as electron relay

• Published in: Chemical physics letters 2017-11, Vol.688, p.11-18
• Main Authors: Zeng, Han, Huo, Wen-Shan, Zhao, Shu-Xian, Zhang, Yu-He
• Format: Article
• Language: English
• Subjects: 3-ferrocenyl dihydropyrazole; Electro-chemical behavior; Electron relay; Laccase; Mediated oxygen reduction
• ISSN: 0009-2614; 1873-4448
• DOI: 10.1016/j.cplett.2017.09.050

Derivative of 3-ferrocenyl dihydropyrazole (FDPFFP) was used as favorable electron relay in application of mediated catalysis to oxygen reduction with quasi-reversible characteristics of electro-chemical reaction and rapid dynamics of electro-reduction for oxidized form of mediator. [Display omitted] •A novel electron mediator on the basis of derivative of pyrazole grafted with ferrocenyl groups, was proposed in the mediated oxygen reduction reaction.•This electron relay showed many advantages such as quasi-reversible characteristics of electron transfer, high formal potential, swift diffusion and rapid dynamics of electron shuttle.•It also displayed apparent catalytic function on oxygen reduction reaction with onset potential at 450 mV vs NHE.•The diffusion of substrate was attributed to be the key factor in restraining the performance of catalysis. Amino group surface tailored multi-wall carbon nano-tubes were covalently tethered to the gold disk electrode and Laccase molecules were covalently coupled to nano-tubes to prepare Lac-based electrode. Derivative of 3-ferrocenyl dihydropyrazole (FDPFFP) was proposed to be electron mediator for mediated oxygen reduction reaction. Investigation in electro-chemical behavior and catalytic performance to enzymatic reaction of FDPFFP indicated that it displayed quasi-reversible characteristics of electro-chemical reaction with rapid dynamics of electron shuttle and had apparent catalytic effect in oxygen reduction (onset potential for catalysis at 450mV vs NHE). This enzymatic catalysis was restrained by the step in diffusion of substrate.