Spectral properties, blue copper

This discussion of copper-containing enzymes has focused on structure and function information for Type I blue copper proteins azurin and plastocyanin, Type III hemocyanin, and Type II superoxide dismutase s structure and mechanism of activity. Information on spectral properties for some metalloproteins and their model compounds has been included in Tables 5.2, 5.3, and 5.7. One model system for Type I copper proteins39 and one for Type II centers40 have been discussed. Many others can be found in the literature. A more complete discussion, including mechanistic detail, about hemocyanin and tyrosinase model systems has been included. Models for the blue copper oxidases laccase and ascorbate oxidases have not been discussed. Students are referred to the references listed in the reference section for discussion of some other model systems. Many more are to be found in literature searches.50... 

The blue copper site exhibits unique spectral properties when compared with those of normal copper complexes. These spectral features include an unusually small copper h perfine splitting of the EPR signal in thej, region (A < 70x10 cm as compared to Aj = 150x10 cm for normal tetragonal copper) [Figure 1] and an... 

Among the coordination compounds obtained on the basis of polypyrazolyl-borates, it is worth emphasizing the copper chelates 235 which are still the only biomimetic model of blue copper proteins, reproducing all their physical (UV-and EPR-spectral) properties [441,446-448], Compound 236 [449] is also an example of complexes of this kind of system ... 

Copper(II) sites in proteins can be classified into three types based on their spectral properties. The blue (Type I) copper proteins are characterised by a visible absorption... 

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