Laccase, a blue copper oxidase, in view of its moderate redox potential can oxidise only phenolic compounds by electron-transfer. However, in the presence of ABTS (2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonate) as a redox mediator, laccase reacts with the more difficult to oxidise non-phenolic substrates, such as benzyl alcohols. The role of ABTS in these mediated oxidations is investigated. Redox interaction with laccase could produce in situ two reactive intermediates from ABTS, namely ABTS++ or ABTS˙+. These species have been independently generated by oxidation with Ce(IV) or Co(III) salts, respectively, and their efficiency as monoelectronic oxidants tested in a kinetic study towards a series of non-phenolic substrates; a Marcus treatment is provided in the case of ABTS++. On these grounds, intervention of ABTS++ as a reactive intermediate in laccase–ABTS oxidations appears unlikely, because the experimental conditions under which ABTS++ is unambiguously generated, and survives long enough to serve as a diffusible mediator, are too harsh (2 M H2SO4 solution) and incompatible with the operation of the enzyme. Likewise, ABTS˙+ seems an intermediate of limited importance in laccase–ABTS oxidations, because this weaker monoelectronic oxidant is unable to react directly with many of the non-phenolic substrates that laccase–ABTS can oxidise. To solve this paradox, it is alternatively suggested that degradation by-products of either ABTS++ or ABTS˙+ are formed in situ by hydrolysis during the laccase–ABTS reactions, and may be responsible for the observed oxidation of non-phenolics.