Bovine cytochrome c (cyt c) was adsorbed on apolycrystalline gold electrode coated with 4-mercaptopyridineand 11-mercapto-1-undecanoic acid self-assembledmonolayers (SAMs) and the thermodynamics and kineticsof the heterogeneous protein-electrode electron transfer(ET) reaction were determined by cyclic voltammetry. TheE0 values for the immobilized protein were found to belower than those for the corresponding diffusing species.The thermodynamic parameters for protein reduction (DH0 rcand DS0 rc) indicate that the stabilization of the ferric statedue to protein–SAM interaction is enthalpic in origin. Thekinetic data suggest that a tunneling mechanism is involvedin the ET reaction: the distance between the redox center ofthe protein and the electrode surface can be efficientlyevaluated using the Marcus equation.
Thermodynamic and Kinetic Aspects of the Electron Transfer Reaction of Bovine Cytochrome c Immobilized on 4-Mercaptopyridine and 11-Mercapto-1-Undecanoic Acid Film / Monari, Stefano; Battistuzzi, Gianantonio; Borsari, Marco; D., Millo; C., Gooijer; G., van der Zwan; Ranieri, Antonio; Sola, Marco. - In: JOURNAL OF APPLIED ELECTROCHEMISTRY. - ISSN 0021-891X. - STAMPA. - 38:(2008), pp. 885-891. [10.1007/s10800-008-9493-7]
Thermodynamic and Kinetic Aspects of the Electron Transfer Reaction of Bovine Cytochrome c Immobilized on 4-Mercaptopyridine and 11-Mercapto-1-Undecanoic Acid Film
MONARI, Stefano;BATTISTUZZI, Gianantonio;BORSARI, Marco;RANIERI, Antonio;SOLA, Marco
2008
Abstract
Bovine cytochrome c (cyt c) was adsorbed on apolycrystalline gold electrode coated with 4-mercaptopyridineand 11-mercapto-1-undecanoic acid self-assembledmonolayers (SAMs) and the thermodynamics and kineticsof the heterogeneous protein-electrode electron transfer(ET) reaction were determined by cyclic voltammetry. TheE0 values for the immobilized protein were found to belower than those for the corresponding diffusing species.The thermodynamic parameters for protein reduction (DH0 rcand DS0 rc) indicate that the stabilization of the ferric statedue to protein–SAM interaction is enthalpic in origin. Thekinetic data suggest that a tunneling mechanism is involvedin the ET reaction: the distance between the redox center ofthe protein and the electrode surface can be efficientlyevaluated using the Marcus equation.
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