Effects of mutations of aspartic acid 63 on the metal-binding properties of the recombinant N-lobe of human serum transferrin

The effects of mutations of aspartic acid 63 on the metal-binding properties of the recombinant N-lobe of human serum transferrin were evaluated through utilization of recombinant DNA technology. Results have shown that aspartic acid position 63 is an important ligand for tight iron binding in transferrin. Furthermore, mutations from Asp to Ser, Glu, Asn, and Ala weakened the ferric iron binding capacity.