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Reoxidation process of reduced cucumber ascorbate oxidase (1.10.3.3) with dioxygen was investigated in detail through absorption, circular dichroic (CD) and electron paramagnetic resonance (EPR) spectra. One of the three type I coppers and the type II copper were reoxidized more rapidly than other type I coppers. The principal active site of ascorbate oxidase was considered to be comprised of one type I, one type II and a pair of type III coppers similarly to the active sites in laccase and ceruloplasmin. Remaining two type I and a pair of type III coppers were also disclosed to contribute to the oxidation of L-ascorbate.
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