The Interaction of Human Hemoglobin with Erythrosin

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Abstract
The interactions of erythrosin with deoxyhemoglobin, HbO2, COHb, methemoglobin, cyanomethemoglobin and Hb .alpha. and .beta. chains were studied by using equilibrium dialysis, the difference and circular dichroic (CD) spectra and stopped-flow methods. The values of equilibrium and kinetic parameters, as well as CD characteristics, show that in addition to a number of weak binding sites, Hb contains 4 relatively strong binding sites, 1 per chain. The properties of the strong binding sites depend on the ligand of the heme group, and the charge of the heme group is not directly responsible for this fact. The properties of deoxyhemoglobin and methemoglobin, differing from the mutually close properties of the other derivatives, confirm that the state of the heme group affects the conformation of Hb molecules in solution. These results are in agreement with the classification established on the heme iron spin state.