Abstract
The organic free radical in galactose oxidase is exchange coupled to the mononuclear copper atom in the active site of the holoenzyme. By removing the copper, the radical can be generated in high concentrations in its electron paramagnetic resonance (EPR)-detectable form. We have carried out a detailed study of the magnetic resonance properties of the radical in the apoenzyme and of a series of phenol model compounds. In the protein, the radical EPR spectrum has partially resolved fine structure with a center crossing at g=2.0055 and an overall peak-to-trough line width of 33 G
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