Analysis of the binding mechanism between o-phenylenediamine and bovine hemoglobin by molecular spectroscopy and molecular modeling methods

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.

Keywords:

• Bovine hemoglobin
• interaction
• molecular docking
• o-phenylenediamine
• spectroscopy

Disclosure statement

The authors declare that they have no conflict of interests.

Author contributions

Jian-li Liu and Yu-chi Kong contributed equally to this work.

Additional information

Funding

This study was supported by the National Natural Science Foundation of China [No.31770017], Project Supported by Scientific Research Fund of Liaoning Provincial Education Department [No. LQN201714], Startup Foundation for Doctors of Liaoning Province [No.20170520258], Project Supported for Youth and Middle-aged Science and Technology Innovative Talents of Shenyang City [No. RC180240].