Reduction thermodynamics of the T1 Cu site in plant and fungal laccases.

BATTISTUZZI, G; BELLEI, M; LEONARDI, A; PIERATTELLI, R; DE CANDIA, A; VILA, AJ ; SOLA, M

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY

SPRINGER

Lugar: Springer Berlin / Heidelberg; Año: 2005 vol. 10 p. 867 - 873

0949-8257

The thermodynamic parameters for reduction of the type-1 (T1) copper site in Rhus vernicifera and Trametes versicolor laccases and for the derivative of the former protein from which the type-2 copper has been selectively removed (T2D) have been determined with UV?vis spectroelectrochemistry. In all cases, the enthalpic term turns out to be the main determinant of the Eo¢ of the T1 site. Also the difference between the reduction potentials of the two laccases is enthalpybased and reflects differences in the coordination features of the T1 sites and their protein environment. The T1 sites in native R. vernicifera laccase and its T2D derivative show the same Eo¢, as a result of compensatory differences in the reduction thermodynamics. This suggests that removal of the type-2 (T2) copper results in modification of the reduction-induced solvent reorganization effects, with no influence in the structure of the multicopper protein site. This conclusion is supported by NMR data recorded on the native, the T2D, and Hgsubstituted T1 derivatives of R. vernicifera laccase, which show that the T1 and T2/T3 sites are largely noninteracting.