Stephen H. Brown

TL;DR: It is speculated that structural differences in the substrate-activation site (a 'blue', type 1 copper center) control the redox potential range as well as substrate specificity, and the cystine content contributes to stability.

TL;DR: The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 Å and is a monomer composed of three cupredoxin-like β-sandwich domains, similar to that found in ascorbate oxidase.

TL;DR: Two laccases have been purified to apparent electrophoretic homogeneity from the extracellular medium of a 2,5-xylidine-induced culture of the white rot basidiomycete Trametes villosa and the purified recombinant protein has the same pI, spectral properties, stability, and pH profiles as the purified native protein.

TL;DR: The deduced amino acid sequence of M. thermophila laccase (MtL) shows homology to laccases from diverse fungal genera and Amino-terminal sequence data suggests that MtL is synthesized as a preproenzyme.

TL;DR: Although the redox potentials were not significantly altered, the Km, kcat and fluoride inhibition of the laccases were greatly changed by the mutations, interpreted as possible mutation-induced structural perturbations on the molecular recognition between the reducing substrate and laccase and on the electron transfer from the substrate to the type-1 Cu centre.