Abstract
The electron paramagnetic resonance (EPR) spectra of type 1 copper(II) in 63Cu-enriched Coriolus versicolor laccase A (benzenediol:oxygen oxidoreductase, EC 1.10.3.2) have been studied. The X-band EPR spectrum in type 2 copper-depleted [ 63Cu]laccase A exhibited well-resolved ligand superhyperfine structure in the g ⊥ region. This structure was assigned to an interaction with two nitrogens and two protons, and assignment which is consistent with a model in which the two nitrogens belong to two histidine ligands an the two protons are the methylene protons of a coordinating cysteine. It also requires the delocalization of a substantial amount of the type 1 copper(II) unpaired electron density onto the cysteine sulphur.
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