pH and solvent H/D isotope effects on the thermodynamics and kinetics of electron transfer for electrode-immobilized native and urea-unfolded stellacyanin

The thermodynamics of Cu(II) to Cu(I) reduction and the kinetics of the electron transfer (ET) process for Rhus vernicifera stellacyanin (STC) immobilized on a decane-1-thiol coated gold electrode have been measured through cyclic voltammetry at varying pH and temperature, in the presence of urea...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 28(2012), 42 vom: 23. Okt., Seite 15087-94
1. Verfasser: Ranieri, Antonio (VerfasserIn)
Weitere Verfasser: Battistuzzi, Gianantonio, Borsari, Marco, Bortolotti, Carlo Augusto, Di Rocco, Giulia, Sola, Marco
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Metalloproteins Plant Proteins Solvents stellacyanin protein, plant 12738-61-3 Gold 7440-57-5 Urea 8W8T17847W
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245 1 0 |a pH and solvent H/D isotope effects on the thermodynamics and kinetics of electron transfer for electrode-immobilized native and urea-unfolded stellacyanin 
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520 |a The thermodynamics of Cu(II) to Cu(I) reduction and the kinetics of the electron transfer (ET) process for Rhus vernicifera stellacyanin (STC) immobilized on a decane-1-thiol coated gold electrode have been measured through cyclic voltammetry at varying pH and temperature, in the presence of urea and in D(2)O. Immobilized STC undergoes a limited conformational change that mainly results in an enhanced exposure of one or both copper binding histidines to solvent which slightly stabilizes the cupric state and increases histidine basicity. The large immobilization-induced increase in the pK(a) for the acid transition (from 4.5 to 6.3) makes this electrode-SAM-protein construct an attractive candidate as a biomolecular ET switch operating near neutral pH in molecular electronics. Such a potential interest is increased by the robustness of this interface against chemical unfolding as it undergoes only moderate changes in the reduction thermodynamics and in the ET rate in the presence of up to 8 M urea. The sensitivity of these parameters to solvent H/D isotope effects testifies to the role of protein solvation as effector of the thermodynamics and kinetics of ET 
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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Gold  |2 NLM 
650 7 |a 7440-57-5  |2 NLM 
650 7 |a Urea  |2 NLM 
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700 1 |a Battistuzzi, Gianantonio  |e verfasserin  |4 aut 
700 1 |a Borsari, Marco  |e verfasserin  |4 aut 
700 1 |a Bortolotti, Carlo Augusto  |e verfasserin  |4 aut 
700 1 |a Di Rocco, Giulia  |e verfasserin  |4 aut 
700 1 |a Sola, Marco  |e verfasserin  |4 aut 
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