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The heme-protein including myoglobin (Mb), hemoglobin (Hb) and horseradish peroxidase (HRP) were immobilized on normal graphite electrode by using N,N-dimethylformamide (DMF). The proteins undergo direct electron-transfer reactions. The current is linearly dependent on the scan rate, indicating that the direct electrochemistry of heme-protein in that case is a surface-controlled electrode process...
Myoglobin (Mb), hemoglobin (Hb) and horseradish peroxidase (HRP) were incorporated in lecithin (PC) film on glassy carbon (GC) electrode by the method of vesicle-fusion. A pair of well-defined and quasi-reversible cyclic voltammetric peaks was obtained, which reflected the direct electron transfer of heme proteins. UV–Vis and reflectance absorption infrared (RAIR) spectroscopy showed that proteins...
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