Direct electrochemistry and electrocatalysis with horseradish peroxidase in Eastman AQ films.
Stable films made from ionomer poly(ester sulfonic acid) or Eastman AQ29 on pyrolytic graphite (PG) electrodes gave direct electrochemistry for incorporated enzyme horseradish peroxidase (HRP). Cyclic voltammetry of HRP-AQ films showed a pair of well-defined, nearly reversible peaks at about -0.33 V vs. SCE at pH 7.0 in blank buffers, characteristic of HRP heme Fe(III)/Fe(II) redox couple. The electron transfer between HRP and PG electrode was greatly facilitated in AQ films. The electrochemical parameters such as apparent heterogeneous electron transfer rate constant (k(s)) and formal potential (E(o')) were estimated by fitting the data of square-wave voltammetry (SWV) with nonlinear regression analysis. Reflectance absorption infrared (RAIR) and UV-Vis absorption spectra demonstrated that HRP retained a near native conformation in AQ films. The embedded HRP in AQ films retained the electrocatalytic activity for oxygen, nitrite and hydrogen peroxide. Possible mechanism of catalytic reduction of H(2)O(2) with HRP-AQ films was proposed.
Huang
R
R
Department of Chemistry, Beijing Normal University, Beijing 100875, China.
Hu
N
N
D002384:Catalysis; D004563:Electrochemistry; D006735:Horseradish Peroxidase / Q000737:chemistry*; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet
D006735:Horseradish Peroxidase