[Study on the interaction between p-HPcZn and myoglobin].
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 X 10(5) and 0.444 respectively. In addition, the interaction can change the conformation of myoglobin markedly also.
Wei
Shao-hua
SH
School of Chemistry and Environmental Science, Jiangsu Key Laboratory of Biofunctional Materials, Nanjing Normal University, Nanjing 210097, China. shwei@njnu.edu.cn
Lu
Shan
S
Ji
Chun
C
Lin
Yun
Y
Zhou
Jia-hong
JH
Shen
Jian
J
D001665:Binding Sites; D005453:Fluorescence; D007211:Indoles / Q000737:chemistry*; D054833:Isoindoles; D009211:Myoglobin / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D015032:Zinc / Q000737:chemistry*
D007211:Indoles; D054833:Isoindoles; D009211:Myoglobin; D015032:Zinc; C013647:phthalocyanine