Abstract
Hemoglobin (Hb) was successfully immobilized in poly(acrylonitrile- co-acrylic acid) (PAN- co-PAA) film modified glassy carbon electrode (GCE). The Hb-PAN- co-PAA film exhibited a pair of well-defined and quasi-reversible cyclic voltammetric peaks for Hb Fe(III)/Fe(II) redox couple in a pH 7.0 phosphate buffer. The formal potential of Hb heme Fe(III)/Fe(II) couple varied linearly with the increase of pH in the range of 4.0–8.0 with a slope of −53.5 mV pH −1, implying that one proton was accompanied with one electron transferred in the electrochemical reaction. Position of Soret absorption band of Hb-PAN- co-PAA film suggested that the Hb kept its secondary structure similar to its native state in the PAN- co-PAA matrix. The protein in PAN- co-PAA matrix acted as a biologic catalyst to catalyze reduction of hydrogen peroxide. The electrocatalytic response showed a linear dependence on the H 2O 2 concentration ranging from 9.2 × 10 −6 to 2 × 10 −3 M with a detection limit of 4.5 × 10 −6 M at 3 σ.
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