Electrochemistry of surface wired redox protein: Axial ligation and control of redox potential

Behera, S.; Raj, C. Retna

doi:10.1016/j.jelechem.2008.04.004

Cited by 3 publications

(2 citation statements)

References 35 publications

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“…W290 can interact by hydrogen bonding with the acetate copper ligand or with the substrate d -galactose, in agreement with model studies , related to the stability and the formal potential of the radical. The difference of 40 mV observed between the redox potential of the tyrosine radical in solution and immobilized on the surface could be associated with the interaction between the carboxylate groups present at the cluster surface with the W290 or due to confinement effects …”

Section: Resultsmentioning

confidence: 99%

“…The difference of 40 mV observed between the redox potential of the tyrosine radical in solution and immobilized on the surface could be associated with the interaction between the carboxylate groups present at the cluster surface with the W290 or due to confinement effects. 27 In the case of the Cu II /Cu I couple, a considerable shift of 115 mV in E°′ is observed. This could be associated with differences in the local dielectric permittivity between reaction in solution and at a surface or, most likely, due to local coordination effects caused by the exchange of the ligand on the copper center from water to the carboxylate group, the latter stabilizing the Cu I formed.…”

Section: Formal Potential Of the Goase Redox Processesmentioning

confidence: 94%

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Direct Electron Transfer to a Metalloenzyme Redox Center Coordinated to a Monolayer-Protected Cluster

et al. 2009

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A strategy for establishing electrical contact to the metal center of a redox metalloenzyme, galactose oxidase (GOase), by coordination of a linker attached to a monolayer-protected gold cluster is presented. The cluster-enzyme hybrid system was first prepared in solution and characterized by high-angle annular dark-field scanning transmission electron microscopy. Electrochemical communication between a gold electrode and GOase was achieved by first modifying the electrode surface with a biphenyl dithiol self-assembled monolayer followed by reaction with gold clusters capped with thioctic acid. GOase was then immobilized by replacement of the H(2)O molecule at the Cu(II) exogenous site by coordination of a carboxylate-terminated gold cluster. This chemical attachment ensured electrical contact between the redox center and the electrode, leading to direct mediatorless electron transfer to the protein. Hybrid systems can find applications in biosensors and biofuel cells and for studying electrochemically the catalytic mechanism of reactions for which free radicals and electron-transfer reactions are involved. The present results can be extended to other metalloenzymes.

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Section: Resultsmentioning

confidence: 99%

Section: Formal Potential Of the Goase Redox Processesmentioning

confidence: 94%

Direct Electron Transfer to a Metalloenzyme Redox Center Coordinated to a Monolayer-Protected Cluster

et al. 2009

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Electrochemical Response of Biomolecules on Carbon Substrates: Comparison between Oxidized HOPG and O-Terminated Boron-Doped CVD Diamond

Baier

Sternschulte

Denisenko

et al. 2011

Nanotechnological Basis for Advanced Sensors

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Functional Interface of Ferric Ion Immobilized on Phosphonic Acid Terminated Self-Assembled Monolayers on a Au Electrode for Detection of Hydrogen Peroxide

et al. 2009

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It is reported that inorganic ferric ion immobilized onto a phosphonic acid terminated functional interface can communicate an electron with the electrode and its electrochemistry is very similar to that of the enzymes (proteins) containing heme groups (such as microperoxidase, horseradish peroxidase, hemoglobin, and myoglobin). For example, its formal potential (E 0 ′) is very close to that of the above-mentioned enzymes (proteins) in neutral solution; analogous to the direct electrochemistry of enzymes (proteins), the formal potential and electron-transfer rate of the immobilized inorganic ferric ion show a strong dependence on solution pH in cyclic voltammetry measurements. In comparison to the traditional enzyme (proteins)-based electrochemical biosensors, the ferric ion modified electrode shows more prominent electrocatalytic activity toward the reduction of hydrogen peroxide due to its high loading, fast electron-transfer rate, and excellent selection toward the reduction of hydrogen peroxide. Importantly, the iron ion, as an inorganic material, is very stable in high temperature and economical to produce. Therefore, the kind of iron ion modified electrode can be used to construct a new generation of biosensors with high performance, and it is very hopeful to substitute for enzyme-based biosensors for detection of hydrogen peroxide.

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Electrochemistry of surface wired redox protein: Axial ligation and control of redox potential

Cited by 3 publications

References 35 publications

Direct Electron Transfer to a Metalloenzyme Redox Center Coordinated to a Monolayer-Protected Cluster

Direct Electron Transfer to a Metalloenzyme Redox Center Coordinated to a Monolayer-Protected Cluster

Electrochemical Response of Biomolecules on Carbon Substrates: Comparison between Oxidized HOPG and O-Terminated Boron-Doped CVD Diamond

Functional Interface of Ferric Ion Immobilized on Phosphonic Acid Terminated Self-Assembled Monolayers on a Au Electrode for Detection of Hydrogen Peroxide

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