Effect of ethanol on functional properties of the human hemoglobin molecule

: The effect of ethanol on the oxygenation of hemoglobin was studied by kinetic absorption spectroscopy. It was found that the efficiency of oxygen geminate rebinding decreased upon ethanol addition. At ethanol concentrations up to 4.5 M, its influence on the structure and functional properties of the hemoglobin molecule is determined by changes in the bulk dielectric constant of solution. The decrease in the rate constant of the bimolecular stage of rebinding k'4 was caused by an increase in the viscosity of solution, with k'4 being approximately 1/eta 0.5. Upon oxidation of hemoglobin to hemichrome initiated by ethanol, dramatic conformational changes in the region of the heme pocket took place. They lead to a more than twofold increase in the efficiency of exit of oxygen molecules from the protein matrix to the solution after photodissociation.