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 E-o' of the T1 site. Also the difference between the reduction potentials of the two laccases is enthalpy-based 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 E-o', 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 Hg-substituted T1 derivatives of R. vernicifera laccase, which show that the T1 and T2/T3 sites are largely noninteracting.

Reduction thermodynamics of the T1 Cu site in plant and fungal laccases / Battistuzzi, Gianantonio; Bellei, Marzia; Leonardi, Alan; R., Pierattelli; Aj, Vila; A., DE CANDIA; Sola, Marco. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 10:(2005), pp. 867-873.

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

BATTISTUZZI, Gianantonio;BELLEI, Marzia;LEONARDI, Alan;SOLA, Marco
2005-01-01

Abstract

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 E-o' of the T1 site. Also the difference between the reduction potentials of the two laccases is enthalpy-based 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 E-o', 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 Hg-substituted T1 derivatives of R. vernicifera laccase, which show that the T1 and T2/T3 sites are largely noninteracting.
10
867
873
Reduction thermodynamics of the T1 Cu site in plant and fungal laccases / Battistuzzi, Gianantonio; Bellei, Marzia; Leonardi, Alan; R., Pierattelli; Aj, Vila; A., DE CANDIA; Sola, Marco. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 10:(2005), pp. 867-873.
Battistuzzi, Gianantonio; Bellei, Marzia; Leonardi, Alan; R., Pierattelli; Aj, Vila; A., DE CANDIA; Sola, Marco
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/305813
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