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http://dx.doi.org/10.5012/bkcs.2007.28.12.2266

Electrochemical Behavior of Redox Proteins Immobilized on Nafion-Riboflavin Modified Gold Electrode  

Rezaei-Zarchi, S. (Institute of Biochemistry and Biophysics, University of Tehran)
Saboury, A.A. (Institute of Biochemistry and Biophysics, University of Tehran)
Hong, J. (Institute of Biochemistry and Biophysics, University of Tehran)
Norouzi, P. (Department of Chemistry, Faculty of Science, University of Tehran)
Moghaddam, A.B. (Department of Chemistry, Faculty of Science, University of Tehran)
Ghourchian, H. (Institute of Biochemistry and Biophysics, University of Tehran)
Ganjali, M.R. (Department of Chemistry, Faculty of Science, University of Tehran)
Moosavi-Movahedi, A.A. (Institute of Biochemistry and Biophysics, University of Tehran)
Javed, A. (Department of Chemistry, University of Agriculture)
Mohammadian, A. (Department of Biotechnology, Faculty of Science, University of Tehran)
Publication Information
Bulletin of the Korean Chemical Society / v.28, no.12, 2007 , pp. 2266-2270 More about this Journal
Abstract
Electron transfer of a redox protein at a bare gold electrode is too slow to observe the redox peaks. A novel Nafion-riboflavin functional membrane was constructed during this study and electron transfer of cytochrome c, superoxide dismutase, and hemoglobin were carried out on the functional membrane-modified gold electrode with good stability and repeatability. The immobilized protein-modified electrodes showed quasireversible electrochemical redox behaviors with formal potentials of 0.150, 0.175, and 0.202 V versus Ag/AgCl for the cytochrome c, superoxide dismutase and hemoglobin, respectively. Whole experiment was carried out in the 50 mM MOPS buffer solution with pH 6.0 at 25 oC. For the immobilized protein, the cathodic transfer coefficients were 0.67, 0.68 and 0.67 and electron transfer-rate constants were evaluated to be 2.25, 2.23 and 2.5 s?1, respectively. Hydrogen peroxide concentration was measured by the peroxidase activity of hemoglobin and our experiment revealed that the enzyme was fully functional while immobilized on the Nafion-riboflavin membrane.
Keywords
Nafion-riboflavin membrane; Cytochrome c; Superoxide dismutase; Hemoglobin; Peroxidase;
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