Abstract：The interaction of p-HPcZn and myoglobin was studied by fluorescence spectra and synchronous fluorescence spectra methods under the physiological condition. The p-HPcZn can quench the fluorescence of myoglobin effectively, and it is indicated that there is a strong interaction occurring between p-HPcZn and myoglobin. The results of the fluorescence spectra with changing temperature proved that the interaction can lead to the formation of complex of p-HPcZn with myoglobin, and quench the fluorescence of myoglobin through the static quenching mechanism. Dealing with the values of fluorescence spectra, the binding parameter and the binding site of the interaction can be obtained, whose values are 2.481×105 and 0.444 respectively. In addition, the interaction can change the conformation of myoglobin markedly also.
魏少华,卢珊.季春,林云,周家宏,沈健*. p-HPcZn与肌红蛋白结合性能的研究[J]. 光谱学与光谱分析, 2008, 28(09): 2148-2151.
WEI Shao-hua, LU Shan, JI Chun, LIN Yun, ZHOU Jia-hong, SHEN Jian*. Study on the Interaction between p-HPcZn and Myoglobin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2008, 28(09): 2148-2151.
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