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Titolo:
Modeling square-wave voltammetry of thin protein films using Marcus theory
Autore:
Saccucci, TM; Rusling, JF;
Indirizzi:
Univ Connecticut, Dept Chem, Storrs, CT 06269 USA Univ Connecticut StorrsCT USA 06269 cut, Dept Chem, Storrs, CT 06269 USA
Titolo Testata:
JOURNAL OF PHYSICAL CHEMISTRY B
fascicolo: 26, volume: 105, anno: 2001,
pagine: 6142 - 6147
SICI:
1520-6106(20010705)105:26<6142:MSVOTP>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; RANGE ELECTRON-TRANSFER; BIOMEMBRANE-LIKE FILMS; LAYER-BY-LAYER; CYTOCHROME-C; CONFORMATIONAL CHANGE; MYOGLOBIN; REDUCTION; ELECTROCHEMISTRY; EQUILIBRIUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Rusling, JF Univ Connecticut, Dept Chem, U-60, Storrs, CT 06269 USA Univ Connecticut U-60 Storrs CT USA 06269 Storrs, CT 06269 USA
Citazione:
T.M. Saccucci e J.F. Rusling, "Modeling square-wave voltammetry of thin protein films using Marcus theory", J PHYS CH B, 105(26), 2001, pp. 6142-6147

Abstract

A model combining Marcus theory with Gaussian distributions of kinetic andthermodynamic parameters was developed for square-wave voltammetry (SWV) and applied to the protein myoglobin in thin films of didodecyldimethylammonium bromide on electrodes. Nonlinear regression analysis allowed direct estimation of electron transfer rate constants and reorganization energies from single experiments at relatively-large pulse heights; Successful fitting relies on the accurate representation of background current within the model. Analysis of 22 voltammograms at pH 6 over a range of frequencies and pulse heights gave-a formal potential consistent with earlier determinations, and a mean log(k(RED)(null)) of 3.3 + 0.8 s(-1), not significantly different from the mean log(k(OX)(null)) of 3.0 +/- 0.6 s(-1). The mean value of reorganization energy lambda (RED) was 0.41 +/- 0.02 eV and lambda (OX) was 0.21 +/- 0.01 eV. Differences in lambda (RED) and lambda (OX) are likely to reflect different solvation, bonding, and conformation near the iron heme regions of MbFe(III) and MbFe(II). Methods presented here promise to be generally applicable to determining Marcus electron-transfer parameters for redox proteins in thin films.

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Documento generato il 05/04/20 alle ore 06:44:20