Study of Electrochemical Behaviour of Myoglobin Using Cyclic Voltammetry and Synchronous Fluorescence Spectroscopy

用循环伏安法和同步荧光光谱技术研究了肌红蛋白的电化学行为，实验结果表明，高铁肌红蛋白分子中至少存在一个可调节分子构象变化的氧分子，而且长时间通入高纯氮气可以除掉高铁肌红蛋白分子内的这个氧，当高铁肌红蛋白分子内的氧被彻底除去后，用循环伏安法可以观察到肌红蛋白在三氧化二铟电极上的准可逆的电学反应。同步荧光光谱实验表明，高铁肌红蛋白在彻底除氧后，分子构象发生了变化，而且这种构象变化是可逆的。Myoglobin undergoes irreversible heterogeneous electron transfer reactions at bare metal electroeds. Thus, much effort has been devoted to obtain quasi-reversible electrochemical reactions of myoglobin at metal electrodes modified with mediators￣(1～3). However, the electron transfer rates at the above modified electrodes is very small so that the spectroelectrochemical techniques should be used in the most of studies. Recently, Taniguchi et al￣[4]. reported that a quasi-reversible electrochemical reaction of the purified horse heart myoglobin was observed at an indium oxide electrode with cyclic voltammetry technique. It was suggested that high purification of myoglobin may be the main reason for obtaining a quasi-reversible electroChemical reaction of myoglobin in the cyclic voltammetry experiments. In this papor, it was reported for the first time that a pair of well-defined redox peaks were oberved in the CV of the commercially available horse heart myoglobin without further purification at an indium oxide electrode after oxygen was eliminated from the solution and the molecules of the oxldized form of myoglobin, i. e.metmyoglobin.作者联系地址：中国科学院长春应用化学研究所电分析开放实验室Author's Address: Laboratory of Electroanalytical Changchun Institute of Applied Chemistry, Chinese Academy of Sciences Changchun, 130022, P. R. Chin