Spectroscopic Studies on the Interaction of Elsinochrome A with Myoglobin
MA Fei1, ZHOU Lin1, WANG Wei1, FENG Yu-ying1, ZHOU Jia-hong1*, WANG Xing-he2*, SHEN Jian1
1. Key Lab of Biofunction Materials of Jiangsu, Analysis and Testing Center, Nanjing Normal University, Nanjing 210046, China 2. Department of Physical Science and Technology, Nanjing Normal University, Nanjing 210046, China
Abstract：The interaction between Elsinochrome A (EA) and myoglobin (Mb) was investigated using UV-Vis and fluorescence spectroscopy. The results suggested that there was a strong interaction between EA and Mb. In the dark, the interaction occurred on the surfaces amidic acid of Mb, but when illuminated, the interactions happened both on amidic acid and the interior structure of hemachrome of Mb. According to the values of the quenching constant, the thermodynamics parameters, the binding constants and the binding sites, it was showed that the binding interaction of EA and Mb was mainly hydrophobic in nature and the quenching mechanism was static quenching procedure. The change in the micro-circumstance of aminos of myoglobin was studied by synchronous fluorescence spectroscopy.
马 菲1，周 林1，王 薇1，冯玉英1，周家宏1*，王兴和2*，沈 健1 . 痂囊腔菌素A与肌红蛋白相互作用的光谱研究 [J]. 光谱学与光谱分析, 2011, 31(06): 1601-1605.
MA Fei1, ZHOU Lin1, WANG Wei1, FENG Yu-ying1, ZHOU Jia-hong1*, WANG Xing-he2*, SHEN Jian1 . Spectroscopic Studies on the Interaction of Elsinochrome A with Myoglobin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2011, 31(06): 1601-1605.
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