期刊
BIOELECTROCHEMISTRY
卷 71, 期 2, 页码 180-185出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2007.04.002
关键词
hemoglobin; carbon black; direct electrochemical reaction; hydrogen peroxide; biocathode
It is reported for the first time that hemoglobin (Hb) was immobilized on the surface of carbon black powders modified at the surface of a glassy carbon electrode. The cyclic voltammetric results showed that the immobilized Hb could undergo a direct quasi-reversible electrochemical reaction. Its formal potential, E-0, is -0.330 V in phosphate buffer solution (pH 6.9) at a scan rate of 100 mV/s and is almost independent of the scan rate in the range of 40-200 mV/s. The dependence of E-0, on the pH of the buffer solution indicated that the conversion of Hb-Fe(III)/Hb-Fe(II) is a one-electron-transfer reaction process coupled with one-proton-transfer. The experimental results also demonstrated that the immobilized Hb retained its bioelectrocatalytic activity for the reduction of H2O2. Furthermore, the immobilized Hb can be stored at 4 degrees C for several weeks without any loss of the enzyme activity. Thus, the immobilized Hb may be used as a biocathodic catalyst in biofuel cells. (c) 2007 Elsevier B.V. All rights reserved.
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