%0 Journal Article
%T Spectroscopic studies on the interaction of hypocrellin A with myoglobin
%A J. H. Zhou
%A X. H. Wu
%A C. Yang
%A X. T. Gu
%A L. Zhou
%A K. X. Song
%A Y. Y. Feng
%A J. Shen
%J Spectroscopy: An International Journal
%D 2007
%I Hindawi Publishing Corporation
%R 10.1155/2007/503537
%X Experimental results of UV-visible absorption spectroscopy and fluorescence spectroscopy indicate that hypocrellin A, which has been studied in photodynamic therapy, can interact with the surface of myoglobin through hydrophobic forces, and form a complex. Based on the Stern¨CVolmer equation, the quenching constants of the process can be calculated to be 4.81¡Á1012 L mol£¿1 s£¿1 (t=25°C) and 4.54¡Á1012 L mol£¿1 s£¿1 (t=42°C) respectively, and the binding constant is 5.53¡Á104 M£¿1 (t=25°C), while the binding sites is 0.94 (t=25°C). In addition, Electron paramagnetic resonance and fluorescence spectroscopic analysis suggests that that the quenching mechanism of the interaction process occurs through the electron transfer between hypocrellin A and myoglobin.
%U http://www.hindawi.com/journals/spectroscopy/2007/503537/abs/