文摘
The isolation and the X-ray crystal structure of physiological copper(II)-L-histidine complex are reported. The neutral five-coordinatecomplex shows distorted square pyramidal geometry with bidentateand tridentate L-histidine ligands. The basic character of thependent imidazole group and H-bonding interactions of bidentateL-histidine ligand are important for copper transport. The uniquestructural features help explain the origin of its thermodynamic stability and kinetic reactivity in human blood along withthe ternary copper(II)-amino acid complexes. The role of L-histidinein interaction with copper(II)-albumin, in cellular uptake of copper,and in treatment of Menkes disease can be studied using theseresults.