Copper GAOX active sites

The intriguing structure of the GAOX active site has raised a challenge to the held of bioinorganic chemistry and inspired the synthesis of an array of molecular models. Models for the isolated Tyr-Cys side chain have yielded important information on the chemistry and spectroscopy of the dissected cofactor, as described earlier (Section VI) (Whittaker <2/., 1993 lioh etal., 1993, 1997 Gerfen <2/., 1996). More recently, attention has been directed at mimicking the complex structure, spectroscopy, and even the catalytic reactivity of the intact radical-copper complex in model chemistry. 

The free radical-copper complex in active GAOX combines two distinct reactive sites to form a two-electron redox unit in the protein with new properties, different from those of the individual components. The... 

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