研究了痂囊腔菌素A(EA)与肌红蛋白(Mb)的相互作用。 通过紫外-可见吸收光谱研究发现痂囊腔菌素A与肌红蛋白在避光与光照两种条件作用模式存在明显差异; 痂囊腔菌素A对肌红蛋白的内源荧光有猝灭作用, 形成了新的配合物, 属于静态猝灭; 热力学计算结果表明痂囊腔菌素A与肌红蛋白之间以疏水作用力结合。 同步荧光光谱研究了痂囊腔菌素A对肌红蛋白二级结构的影响。

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.