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

Ji, Xueping; Jin, Baokang; Jin, Jiye; Nakamura, Toshio

doi:10.1016/j.jelechem.2006.03.011

Cited by 19 publications

(19 citation statements)

References 47 publications

(61 reference statements)

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“…Previous studies of intramolecular electron transfer (ET) in CytC used both spectroscopic (1-6) and electrochemical measurements (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20). In the latter studies, where the rate of ET between the intrinsic redox site and a working electrode has been probed, the CytC was usually attached (covalently or electrostatically) to one electrode via a linker molecule to form a monolayer.…”

mentioning

confidence: 99%

Solid-state electron transport via cytochrome c depends on electronic coupling to electrodes and across the protein

Amdursky

Ferber

Bortolotti

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Electronic coupling to electrodes, Γ, as well as that across the examined molecules, H, is critical for solid-state electron transport (ETp) across proteins. Assessing the importance of each of these couplings helps to understand the mechanism of electron flow across molecules. We provide here experimental evidence for the importance of both couplings for solid-state ETp across the electron-mediating protein cytochrome c (CytC), measured in a monolayer configuration. Currents via CytC are temperature-independent between 30 and ∼130 K, consistent with tunneling by superexchange, and thermally activated at higher temperatures, ascribed to steady-state hopping. Covalent protein-electrode binding significantly increases Γ, as currents across CytC mutants, bound covalently to the electrode via a cysteine thiolate, are higher than those through electrostatically adsorbed CytC. Covalent binding also reduces the thermal activation energy, E a , of the ETp by more than a factor of two. The importance of H was examined by using a series of seven CytC mutants with cysteine residues at different surface positions, yielding distinct electrode-protein(-heme) orientations and separation distances. We find that, in general, mutants with electrode-proximal heme have lower E a values (from high-temperature data) and higher conductance at low temperatures (in the temperatureindependent regime) than those with a distal heme. We conclude that ETp across these mutants depends on the distance between the heme group and the top or bottom electrode, rather than on the total separation distance between electrodes (protein width).bioelectronics | temperature dependence | protein conduction

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mentioning

confidence: 99%

Solid-state electron transport via cytochrome c depends on electronic coupling to electrodes and across the protein

Amdursky

Ferber

Bortolotti

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…11 A pair of well-defined quasi-reversible redox peaks occurred. The formal potential, E˚¢, taken as the average of Epc and Epa, was -0.032 V, with DEp, the peak-to-peak potential separation of anodic and cathodic waves, being 0.010 V in 10 mM PBS (pH 7.0) at a scan rate of 40 mV s -1 .…”

Section: Electrochemistry Of Cyt C Immobilized On Binary Samsmentioning

confidence: 98%

Amperometric Sensor for Hydrogen Peroxide Based on Immobilized Cytochrome c on Binary Self-assembled Monolayers

Nakamura

2009

ANAL. SCI.

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“…[25][26][27] Recently the construction of binary self-assembled monolayers (SAMs) of thioctic acid (T-COOH) and thioctic amide (T-NH2) modified electrodes was reported. 28 The voltammetry of immobilized cytochrome c (cyt c) on the modified electrode and the application to the biosensing of metabolismic materials in nonaqueous solution systems were also described. 28,29 2 Tyrosinase Immobilized PAA Membrane…”

Section: Introductionmentioning

confidence: 99%

“…28 The voltammetry of immobilized cytochrome c (cyt c) on the modified electrode and the application to the biosensing of metabolismic materials in nonaqueous solution systems were also described. 28,29 2 Tyrosinase Immobilized PAA Membrane…”

Section: Introductionmentioning

confidence: 99%

Electrochemical Biosensors in Nonaqueous Solutions and Their Applications

Nakamura

2007

ANAL. SCI.

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This review first describes the invention of functional interfaces to promote biochemical redox reactions between substrates in dipolar aprotic solvents and enzymes or related compounds immobilized at the interface. The interfaces contain hydrophilic polymer membranes, a gold nanoparticle self-assembled electrode constructed by using rigid rod dithiols, and binary self-assembled monolayers composed of amino and carboxyl terminal groups. Other topics covered are: the electrochemical characterization of the hydrophilic polymer membrane; the development of biosensors to obtain reaction parameters of enzymatic and of electrochemical kinetics; and applications to the study of materials involved in metabolism.

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

Cited by 19 publications

References 47 publications

Solid-state electron transport via cytochrome c depends on electronic coupling to electrodes and across the protein

Solid-state electron transport via cytochrome c depends on electronic coupling to electrodes and across the protein

Amperometric Sensor for Hydrogen Peroxide Based on Immobilized Cytochrome c on Binary Self-assembled Monolayers

Electrochemical Biosensors in Nonaqueous Solutions and Their Applications

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