In this study, we investigated the possibility of interactions between the solvent molecules with the Heme group in the human hemoglobin. The results of this study answer a key question: whether the interactions of the Heme unit with its surroundings are interdependent or independent of the protein units of human hemoglobin. Contributions of the intermolecular interactions were determined by exploiting the solvatochromism spectroscopic data by Kamlet-Taft (KAT) polarity functions. Solvent polarity effects on the nonlinear properties of the Heme's groups in the human hemoglobin (Hb) were investigated via the Z-scan method. The experimental results obtained with spectroscopic and nonlinear optical parameters (absorption coefficient and refractive index) show that the mechanism of solvation and the interactions of Heme are controlled by suitable configuration of the protein units of hemoglobin. In other words, interactions of the Heme with α- and β-globins are an effective factor in controlling the optical behavior of Heme.
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| http://dx.doi.org/10.1016/j.saa.2020.118855 | DOI Listing |
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