Artificial enzymes copper complexes

This paper summarizes briefly the physicochemistry and enzymology of plant copper oxidases with particular emphasis on polyphenol oxidase and laccase. A brief comparative discussion of other naturally occurring copper proteins and artificial copper proteins is appropriate when discussing the physicochemistry of the copper site itself. In the case of the copper proteins listed in Table I, we know a great deal more about the copper site than about the physicochemistry of the rest of the protein molecule. This is primarily a result of the availability of sophisticated spectroscopic techniques such as optical spectroscopy (both absorption and circular dichroism) and electron spin resonance which are applicable to the electronic transitions of the copper ion. On the other hand, protein chemistry has progressed more slowly. Many of the proteins are large and complex multisubunit enzymes, difficult to purify, and often unstable. There are several excellent reviews on this group of proteins (59, 60, 61, 62). 

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