Fluorescence spectroscopic investigation of the interaction between benzidine and bovine hemoglobin

The interaction of benzidinne (BZ) with bovine hemoglobin (BHb) under physilolgical condition was studied by fluorescence spectrum. Fluorescence data revealed that the fluorescence quenching of BHb by BZ was the result of the formed complex of BZ–BHb, The quenching and energy transfer mechanisms were discussed, respectively. The binding constants and thermodynamic parameters at three different temperatures, the binding locality, and the binding power were obtained. The hydrophobic and hydrogen bonds interactions were the predominant intermolecular forces to stabilize the complex. The conformation of BHb was discussed by synchronous and three-dimensional fluorescence techniques.