Redox reaction of myoglobin at a benzimidazole‐modified silver electrode

Benzimidazole could be attached to a silver electrode by a covalent bonding method to give a high stable chemically modified electrode. Not only was the modified electrode electroactive, myoglobin could also undergo redox reactions at the surface of the electrode. In 0.20 mol/L NaAc‐HAc buffer (pH 5.5), the benzimidazole modified electrode gave a pair of redox waves with a cathodic peak potential E pc of 0.10V and an anodic peak potential E pa of 0.25 V. On addition of myoglobin to the buffer, the peaks all increased due to the redox processes of the protein. In addition, comparison studies of the purified protein with the commercial sample revealed that myoglobin could still give electrode response even though it had not been previously purified. Therefore, benzimidazole modified silver electrode might be very attractive for the electrochemical studies of myoglobin.