Study of the Interaction of Hemoglobin with Ligands from Resonance Raman Spectra

By the method of resonance Raman spectroscopy the equilibrium between liganded (HbL) and deliganded (Hb) forms of human hemoglobin is studied in destabilization of the solvate protein shell by introducing a cosolvent in the solution. It is shown that the introduction of ethanol leads to a nearly fivefold decrease in the ligand affinity of hemoglobin detected from the increase in the intensity of the 1355 cm^–1 ₄ line. The conformation of the heme and of the hemic pocket remains constant on addition of ethanol to the solution. Owing to the short time spent on measurement, this method can be used for a rapid evaluation of the influence of various preparations on the ligand affinity of hemoglobin.