Investigation of Diuron Effect as an Environmental Pollution on the Structure and Stability of Human Hemoglobin

Abstract Diuron is being used as an herbicide in agricultural crops and non-crops areas such as roads, garden paths, and railway lines. According to clinical studies, it is slightly toxic to mammals, birds and human health. In this study, the intermolecular interaction of Diuron and human hemoglobin was investigated using various spectroscopic methods. The UV-visible and fluorescence results showed that the Diuron binds to Hb. According to the linear S-V plot, dynamic enhancement constant reduced with rising of temperature. Diuron formed a complex with HHb by static mechanism of enhancement and changed the conformation of Hb. The thermodynamic result suggested that the binding reaction was spontaneous and exothermic. Also, the result of synchronous fluorescence, heme degradation, thermal denaturation, aggregation and determination of surface hydrophobicity indicated that the Diuron could induce the conformational alteration, unfolding and heme degradation of Hb. bioanformatics study used for deciphering the binding location of a ligand to a biomicromolecules. According to molecular docking results the Diuron binds near the hydrophobic pocket of Hb which hydrophobic residue was located in this region.