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

被引:21
作者
Battistuzzi, G
Bellei, M
Leonardi, A
Pierattelli, R
De Candia, A
Vila, AJ
Sola, M
机构
[1] Univ Modena & Reggio Emilia, Ctr SCS, Dept Chem, I-41100 Modena, Italy
[2] Univ Florence, CERM, I-50019 Florence, Italy
[3] Univ Florence, Dept Chem, I-50019 Florence, Italy
[4] Univ Nacl Rosario, CONICET, Inst Biol Mol & Celular Rosario, Div Mol Biol, RA-2002 Rosario, Argentina
[5] Univ Nacl Rosario, Fac Ciencias Bioquim & Farmaceut, Biophys Sect, RA-2002 Rosario, Argentina
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2005年 / 10卷 / 08期
关键词
laccases; multi-copper oxidases; redox enzymes; spectroelectrochemistry; NMR;
D O I
10.1007/s00775-005-0035-z
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:867 / 873
页数:7
相关论文
共 70 条
[1]  
Banci L, 2002, ADV PROTEIN CHEM, V60, P397
[2]   Redox thermodynamics of blue copper proteins [J].
Battistuzzi, G ;
Borsari, M ;
Loschi, L ;
Righi, F ;
Sola, M .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (03) :501-506
[3]   Redox thermodynamics, acid-base equilibria and salt-induced effects for the cucumber basic protein. General implications for blue-copper proteins [J].
Battistuzzi, G ;
Borsari, M ;
Loschi, L ;
Sola, M .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 1997, 2 (03) :350-359
[4]   Ligand loop effects on the free energy change of redox and pH-dependent equilibria in cupredoxins probed on amicyanin variants [J].
Battistuzzi, G ;
Borsari, M ;
Canters, GW ;
di Rocco, G ;
de Waal, E ;
Arendsen, Y ;
Leonardi, A ;
Ranieri, A ;
Sola, M .
BIOCHEMISTRY, 2005, 44 (29) :9944-9949
[5]   Characterization of the solution reactivity of a basic heme peroxidase from Cucumis sativus [J].
Battistuzzi, G ;
Bellei, M ;
Bortolotti, CA ;
Di Rocco, G ;
Leonardi, A ;
Sola, M .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2004, 423 (02) :317-331
[6]   Enthalpy/entropy compensation phenomena in the reduction thermodynamics of electron transport metalloproteins [J].
Battistuzzi, G ;
Borsari, M ;
Di Rocco, G ;
Ranieri, A ;
Sola, M .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2004, 9 (01) :23-26
[7]   1H NMR of native and azide-inhibited laccase from Rhus vernicifera [J].
Battistuzzi, G ;
Di Rocco, G ;
Leonardi, A ;
Sola, M .
JOURNAL OF INORGANIC BIOCHEMISTRY, 2003, 96 (04) :503-506
[8]   Control of metalloprotein reduction potential: Compensation phenomena in the reduction thermodynamics of blue copper proteins [J].
Battistuzzi, G ;
Bellei, M ;
Borsari, M ;
Canters, GW ;
de Waal, E ;
Jeuken, LJC ;
Ranieri, A ;
Sola, M .
BIOCHEMISTRY, 2003, 42 (30) :9214-9220
[9]   Redox thermodynamics of the Fe3+/Fe2+ couple in horseradish peroxidase and its cyanide complex [J].
Battistuzzi, G ;
Borsari, M ;
Ranieri, A ;
Sola, M .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (01) :26-27
[10]   Enthalpic and entropic contributions to the mutational changes in the reduction potential of azurin [J].
Battistuzzi, G ;
Borsari, M ;
Canters, GW ;
de Waal, E ;
Loschi, L ;
Warmerdam, G ;
Sola, M .
BIOCHEMISTRY, 2001, 40 (23) :6707-6712