Thermal stability of hemoglobin and myoglobin: effect of spin states.
The thermal stability of various methemoglobin and metmyoglobin derivatives at different ligand concentrations and pH were studied by the method of differential scanning calorimetry. Comparing to water as a ligand, cyanide and azide are most effective in protecting the protein; fluoride stabilizes the protein slightly whereas imidazole and thiocyanate have little effect. Assuming thermal denaturation can be described by an activated two-state process, the activation parameters of all the derivatives were determined. We have also found that the stability of hemoglobin and myoglobin does not correlate with the iron atom spin state but depends instead on steric interactions with the ligands. On the reasonable assumption that structure and stability are related, this implies a definite dependence of structure on steric interactions.
D002152:Calorimetry, Differential Scanning; D006454:Hemoglobins; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007501:Iron; D009211:Myoglobin; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
D006454:Hemoglobins; D009211:Myoglobin; D007501:Iron