The chemical biology of copper.
Major progress was made in 1997 in the understanding of the biological transport of copper. Blue copper and CuA sites have very low electron transfer reorganization energies. The mechanisms of copper-containing oxygenases and oxidases have been clarified by recent crystal structure determinations. Protein folding has been shown to tune the reduction potentials of blue copper proteins by hydrophobic encapsulation of the active sites and strict control of the axial ligation.
Göteborg University, Department of Chemistry, Biochemistry and Biophysics, PO Box 462, SE-405 30, Göteborg, Sweden. bgm@bcbp.gu.se
B G
BG
Malmström
J
J
Leckner
D001400:Azurin / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites / Q000502:physiology; D001692:Biological Transport / Q000502:physiology; D003300:Copper / Q000737:chemistry / Q000502:physiology*; D005656:Fungal Proteins / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D010105:Oxygenases / Q000737:chemistry; D017510:Protein Folding
D001426:Bacterial Proteins; D005656:Fungal Proteins; D008667:Metalloproteins; D001400:Azurin; D003300:Copper; D010088:Oxidoreductases; D010105:Oxygenases