Controlling Interfacial Electron-Transfer Kinetics of Cytochrome <i>c</i> with Mixed Self-Assembled Monolayers

Kasmi, Asma El; Wallace, Jean Marie; Bowden, Edmond F.; Binet, Sophie; Linderman, Russell J.

doi:10.1021/ja973417m

Cited by 237 publications

(257 citation statements)

References 20 publications

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“…The electrochemical response of cyt c immobilized on binary SAMs composed of COOH/OH [15,16] and COOH/CH 3 [17,18] terminated alkanethiols were improved obviously, compared to that observed for cyt c immobilized on the single-component COOH SAMs.…”

Section: Introductionmentioning

confidence: 74%

“…This is attributed to a larger Gibbs energy of folding of the reduced form than that of the oxidized form [37]. On the other hand, the shift might arise from the unfolding of cyt c, especially for oxidized form of cyt c due to enhanced electronic coupling on the cyt c/SAMs interface [38].…”

Section: Electrostatic Interactions Of T-cooh+t-nh 2 |Au With Cyt Cmentioning

confidence: 99%

“…Based on previous studies [13][14][15][16][17][18], we found that different types of monolayer surface could exert effects on the extent of adsorption and electrochemical behavior of cyt c. Although alkanethiols with different chain lengths were used for COOH/OH and COOH/CH 3 terminated SAMs, the stability of the SAMs and effective electron transfer couldn't be improved at the same time. Longer-chain alkanethiols SAMs were more stable due to stronger Van der Waals forces among longer-chain alkanethiols, whereas much slower electron transfer rate was obtained due to an increase in electron transfer distance [19,20].…”

Section: Introductionmentioning

confidence: 99%

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Voltammetry of immobilized cytochrome c on novel binary self-assembled monolayers of thioctic acid and thioctic amide modified gold electrodes

Jin

et al. 2006

Journal of Electroanalytical Chemistry

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Horse heart cytochrome c (cyt c) was adsorbed on the binary self-assembled monolayers (SAMs) composed of thioctic acid (T-COOH) and thioctic amide (T-NH 2 ) at gold electrodes via electrostatic interaction. The cyt c adsorbed on the modified gold electrode exhibited well-defined reversible electrochemical behavior in 10 mM phosphate buffer solution (PBS, pH 7.0). The surface concentration (Г) of electroactive species, cyt c, on the binary SAMs was higher than that in single-component SAMs of T-COOH, and reached a maximum value of 9.2×10 -12 mol cm -2 when the ratio of T-COOH to T-NH 2 in adsorption solution was of 3:2, and the formal potential

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Section: Introductionmentioning

confidence: 74%

Section: Electrostatic Interactions Of T-cooh+t-nh 2 |Au With Cyt Cmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Voltammetry of immobilized cytochrome c on novel binary self-assembled monolayers of thioctic acid and thioctic amide modified gold electrodes

Jin

et al. 2006

Journal of Electroanalytical Chemistry

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“…Γ, C dl , and I values (table S1) were normalized to the geometric electrode surface area (A geo , 0.246 cm 2 ). Γ values for copper, 6-(ferrocenyl)hexanethiol (FcHxSH) and cytochrome c were obtained by integration of the anodic current and converted to % monolayer coverage using theoretical Γ values of 2000, 450, and 15 pmol cm -2 for complete monolayer coverage of Cu 27 , FcHxSH, 28 and cyt c, 29 respectively. A real values were determined by multiplying A geo by R f .…”

Section: Methodsmentioning

confidence: 99%

Characterization of Nanoporous Gold Electrodes for Bioelectrochemical Applications

Scanlon¹,

Salaj-Kośla²,

Belochapkine³

et al. 2011

Langmuir

100

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ABSTRACT. The high surface areas of nanostructured electrodes can provide for significantly enhanced surface loadings of electroactive materials. The fabrication and characterisation of nanoporous gold (np-Au) substrates as electrodes for bioelectrochemical applications is described.Robust np-Au electrodes were prepared by sputtering a gold-silver alloy onto a glass support and subsequent de-alloying of the silver component. Alloy layers were prepared with either a uniform or non-uniform distribution of silver and, post de-alloying, showed clear differences in morphology on characterisation with scanning electron microscopy. Redox reactions under kinetic control, in particular measurement of the charge required to strip a gold oxide layer, provided the most accurate measurements of the total electrochemically addressable electrode surface area, A real .Values of A real up to 28 times that of the geometric electrode surface area, A geo , were obtained. For diffusion controlled reactions overlapping diffusion zones between adjacent nanopores established limiting semi-infinite linear diffusion fields where the maximum current density was dependent on A geo . The importance of measuring the surface area available for the immobilisation was determined 2 using the redox protein, cyt c. The area accessible to modification by a biological macromolecule, A macro , such as cyt c was reduced by up to 40 % compared to A real , demonstrating that the confines of some nanopores were inaccessible to large macromolecules due to steric hindrances. Preliminary studies on the preparation of np-Au electrodes modified with osmium redox polymer hydrogels and Myrothecium verrucaria bilirubin oxidase (MvBOD) as a biocathode were performed; current densities of 500 A cm -2 were obtained in unstirred solutions.

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“…The possibility of studying the electrochemical features of different electrolytes at lowered temperatures attracts also huge attention in the fields of lithium-ion batteries [2,14]. The low temperature voltammetry is currently seen as a powerful alternative to fast-scan protein-film voltammetry [6,[15][16][17]. By performing experiments in partially organic solvent mixtures at temperatures lower than −90°C, one can slow down the chemical reactions associated with electron transfer at the protein redox active sites and study these reactions using slower scan-rates [9].…”

Section: Introductionmentioning

confidence: 99%

Protein-film voltammetry: A theoretical study of the temperature effect using square-wave voltammetry

Gulaboski

Lovrić²,

Mirčeski³

et al. 2008

Biophysical Chemistry

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Square-wave voltammetry of surface redox reactions is considered as an adequate model for a protein-film voltammetric setup. Here we develop a theoretical approach to analyze the effects of temperature on squarewave voltammograms. The performed simulations address the surface redox reactions featuring slow, modest and fast electron transfer. The theoretical calculations show that the temperature affects the squarewave voltammetric responses in a complex way resulting in a variety of peak shapes. Temperature effects on the phenomena known as "quasireversible maximum" and "split SW peaks" are also analyzed. The simulated results can be used to analyze the redox mechanisms and kinetic parameters of electron transfer reactions in protein-film criovoltammetry and other surface-confined redox systems. Our analysis also shows how "abnormal" features present in some square-wave voltammetric studies can easily be misinterpreted by postulating "multiple species", "stable radicals", or additional processes. Finally we provide a simple algorithm to use the "quasireversible maximum" to determine the activation energy of electron transfer reactions by surface redox systems.

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Controlling Interfacial Electron-Transfer Kinetics of Cytochrome c with Mixed Self-Assembled Monolayers

Cited by 237 publications

References 20 publications

Voltammetry of immobilized cytochrome c on novel binary self-assembled monolayers of thioctic acid and thioctic amide modified gold electrodes

Voltammetry of immobilized cytochrome c on novel binary self-assembled monolayers of thioctic acid and thioctic amide modified gold electrodes

Characterization of Nanoporous Gold Electrodes for Bioelectrochemical Applications

Protein-film voltammetry: A theoretical study of the temperature effect using square-wave voltammetry

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