X-ray structure of physiological copper(II)-bis(L-histidinato) complex.
The isolation and the X-ray crystal structure of physiological copper(II)-L-histidine complex are reported. The neutral five-coordinate complex shows distorted square pyramidal geometry with bidentate and tridentate L-histidine ligands. The basic character of the pendent imidazole group and H-bonding interactions of bidentate L-histidine ligand are important for copper transport. The unique structural features help explain the origin of its thermodynamic stability and kinetic reactivity in human blood along with the ternary copper(II)-amino acid complexes. The role of L-histidine in interaction with copper(II)-albumin, in cellular uptake of copper, and in treatment of Menkes disease can be studied using these results.
Deschamps
Patrick
P
Department of Structural Biology and Biochemistry, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.
Kulkarni
Prasad P
PP
Sarkar
Bibudhendra
B
D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D008024:Ligands; D007706:Menkes Kinky Hair Syndrome / Q000378:metabolism / Q000628:therapy; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000737:chemistry* / Q000378:metabolism
D008024:Ligands; D009942:Organometallic Compounds; C045576:copper bis(histidinate); D006639:Histidine; D003300:Copper