Abstract This study was aimed to reveal the binding mechanism between bovine hemoglobin and o-phenylenediamine by using molecular spectroscopy techniques and molecular modeling methods. The experimental results revealed that the fluorescence quenching mechanism was a combined dynamic and static quenching. The binding constant was (1.17 ± 0.02)×104 L/mol, and only a single binding site exists. The binding distance was 2.46 nm. The binding process was a spontaneous reaction, dominated by hydrophobic forces. The molecular docking simulations have also confirmed the results of the spectroscopic methods. The results reported here may significantly help understanding the interaction mechanism of o-phenylenediamine and hemoglobin.

中文翻译：

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用分子光谱和分子建模方法分析邻苯二胺与牛血红蛋白的结合机制

摘要 本研究旨在利用分子光谱技术和分子建模方法揭示牛血红蛋白与邻苯二胺的结合机制。实验结果表明，荧光猝灭机制是一种动态猝灭和静态猝灭相结合的机制。结合常数为（1.17±0.02）×104 L/mol，仅存在一个结合位点。结合距离为2.46 nm。结合过程是自发反应，由疏水力主导。分子对接模拟也证实了光谱方法的结果。这里报告的结果可能对理解邻苯二胺和血红蛋白的相互作用机制有很大帮助。