ABSTRACT
This chapter provides the chemical and physicochemical properties of the amine oxidases (AO) copper, as compared to the copper of other copper proteins. On the basis of the evidence so far available for AOs from various sources, copper is the only inorganic cofactor known for these enzymes and is reproducibly present in all enzyme preparations as 2 g-atoms per mole of protein, likely to be one copper for each subunit of enzyme. The AO copper seems to have a rather low redox potential and is rather inert kinetically in redox reactions. An interesting feature of substrate-perturbed EPR spectra of AOs is that in the beef plasma enzyme a reaction of only half the copper sites has been demonstrated by 35-GHz EPR analysis. The most complicated case of ligand interaction with AOs is that of the well known metal chelating agent, diethyldithiocarbamate.
