期刊
BIOELECTROCHEMISTRY
卷 71, 期 2, 页码 198-203出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2007.04.007
关键词
direct electrochemistry; hemoglobin; polyacrylonitrile; electrocatalysis
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.
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