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The effects of single amino acid substitution on the thermal stability of the N-terminal half-molecule of human transferrin and its iron-binding affinity have been studied by high-sensitivity scanning calorimetry. All site-directed mutations are located on the surface of the binding cleft, and they are D63--&gt;S, D63--&gt;C, G65--&gt;R, H207--&gt;E and K206--&gt;Q. Differential scanning calorimetry results show that the mutations do not significantly alter the conformational stability of the apo-forms of the proteins. The changes in free energy of unfolding relative to the wild-type protein range from 0.83 to -2.4 kJ/mol. The D63--&gt;S, G54--&gt;R and H207--&gt;E mutations slightly destabilize the apo-protein, while the D63--&gt;C and K206--&gt;Q mutations increase its stability by a small amount. However, there are large compensating enthalpy-entropy changes caused by all mutations. All mutants bind ferric ion, but with different affinities. Replacement of Asp-63 by either Ser or Cys decreases the apparent binding constant by 5-6 orders of magnitude. The G65--&gt;R mutation also decreases the apparent binding constant by 5 orders of magnitude. The K206--&gt;Q mutation increases the apparent binding constant by 20-fold, while the H207--&gt;E mutation does not significantly change the apparent iron-binding affinity of the half-molecule.

Calorimetric studies of the N-terminal half-molecule of transferrin and mutant forms modified near the Fe3+-binding site