Studies on direct electron transfer and biocatalytic properties of hemoglobin in polyracrylonitrile matrix

The direct electrochemistry of hemoglobin (Hb) immobilized in polyacrylonitrile (PAN) modified glassy carbon electrode was described. The protein-PAN 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 5.0-9.0 with a slope of 54 mV pH(-1) 1, which implied that a proton transfer was accompanied with each electron transfer in the electrochemical reaction. Position of Sorel absorption band of Hb-PAN film suggested that the Hb kept its secondary structure similar to its native state in the PAN matrix. The Hb in PAN matrix acted as a biologic catalyst to catalyze the reduction of hydrogen peroxide. The electrocatalytic response showed a linear dependence on the H2O2 concentration ranging ftom 8.3 x 10(-6) to 5x 10(-4) mol L-(1) with a detection limit of 8.3 x 10(-6) mol L-1 at 3 sigma. The apparent Michaelis-Menten constant K-M(app) for H2O2 sensor was estimated to be 0.9 mmol L-1 (c) 2007 Elsevier B.V. All rights reserved.