This paper describes electrochemical behavior of laccase from the fungus Trametes versicolor. The issues related to discrimination of the redox potentials corresponding to copper centers T1 and T2/T3 in the active site and possible mechanism of intramolecular electron transfer have been discussed. The electron-transfer rate constant for laccase immobilized on carbon electrode is 3.4 s−1. The bioelectrocatalytic activity of the enzyme was studied in the presence of 1,4-hydroquinone (HQ). The kinetics of HQ oxidation is very fast (KM=3.8 μM). However, the catalytic activity of laccase in the presence of high concentration of HQ decreases drastically. It is suggested that the T2/T3 copper center is able to accept electrons from HQ molecules directly via intramolecular channel.