Bio-mimicking galactose oxidase and hemocyanin, two dioxygen-processing copper proteins.
The modelling of the active sites of metalloproteins is one of the most challenging tasks in bio-inorganic chemistry. Copper proteins form part of this stimulating field of research as copper enzymes are mainly involved in oxidation bio-reactions. Thus, the understanding of the structure-function relationship of their active sites will allow the design of effective and environmental friendly oxidation catalysts. This perspective illustrates some outstanding structural and functional synthetic models of the active site of copper proteins, with special attention given to models of galactose oxidase and hemocyanin.
Gamez
Patrick
P
Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Koval
Iryna A
IA
Reedijk
Jan
J
D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004247:DNA / Q000737:chemistry; D005692:Galactose Oxidase / Q000737:chemistry*; D006433:Hemocyanins / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D018716:Molecular Mimicry; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*
D008024:Ligands; D003300:Copper; D004247:DNA; D006433:Hemocyanins; D005692:Galactose Oxidase; D010100:Oxygen