Recent developments in faradaic bioelectrochemistry

Armstrong, Fräser A.; Wilson, George S.

doi:10.1016/s0013-4686(00)00342-x

Cited by 473 publications

(350 citation statements)

References 150 publications

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“…Indeed, reports of the direct electrochemistry of any other dinuclear iron containing protein have been sparse, with the soluble methane monooxygenase being the sole example (45,46). The advantages of the direct electrochemical techniques described herein over mediated potentiometric or microcoulometric titrations are many (35). Rapid data acquisition using cyclic voltammetry is possible enabling the study of a wide range of pH values to be undertaken with the same aliquot of protein solution within a short time interval (∼60 min).…”

Section: Discussionmentioning

confidence: 99%

“…The labile ferrous ion in Uf r has been replaced by other divalent metal ions such as Mn, Co, Ni, Cu, and Zn (20,28,31,32), with retention of phosphatase activity. The ferric ion has been replaced by analogues such as Al III and Ga III to generate catalytically active enzymes, whereas the In III analogue was inactive (33 (35). Typically, the protein is immobilized within a thin film coated onto the working electrode surface where heterogeneous electron transfer may take place without diffusion control.…”

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confidence: 99%

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Direct Electrochemistry of Porcine Purple Acid Phosphatase (Uteroferrin)

2004

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Cyclic voltammetry of the non-heme diiron enzyme porcine purple acid phosphatase (uteroferrin, Uf) has been reported for the first time. Totally reversible one-electron oxidation responses (Fe III-Fe II f Fe III-Fe III ) are seen both in the absence and in the presence of weak competitive inhibitors phosphate and arsenate, and dissociation constants of these oxoanion complexes formed with uteroferrin in its oxidized state (Uf o ) have been determined. The effect of pH on the redox potentials has been investigated in the range 3 < pH < 6.5, enabling acid dissociation constants for Uf o and its phosphate and arsenate complexes to be calculated.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Direct Electrochemistry of Porcine Purple Acid Phosphatase (Uteroferrin)

2004

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“…Among redox proteins, cytochrome c (cyt c) is probably one of the most extensively explored compound due to its key role in the respiratory chain [7][8][9][10][11][12][13] . Cyt c is a water soluble heme protein, with spherical shape and near 3 nm in diameter, which has the function of accepting electrons from cyt c reductase and delivering them to cyt c oxidase in the mitochondrial inner-membrane 14 .…”

Section: Introductionmentioning

confidence: 99%

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

et al. 2017

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The direct electron transfer (DET) to redox proteins has become a central topic in the development of biotechnological devices. The present work explores the mechanisms of the direct electrochemistry between cytochrome c and a conducting polymer, PEDOT-PSS. This polymer has been electrosynthesized from its monomers in aqueous solution on gold electrodes and its capabilities for DET to cyt c have been examined by electrochemical and spectroelectrochemical methods. The polymer was electrodeposited with controlled thickness and we determined the electron transfer rate constant for cyt c oxidation was about 2 orders of magnitude higher than those obtained at conventional electrodes. Spectroelectrochemical measurements allowed to evaluate the redox state of the polymer as a function of the potential and, in addition, the observation of intrinsic cyt c redox activity upon electron transfer from the conducting polymer. During the oxidation process of this protein, lysine residues placed near the heme crevice interact electrostatically with the anionic polyelectrolyte PSS. This interaction favors the orientation of the heme group towards the chains of PEDOT backbone, which is the eventual responsible for the electron transfer to the protein.3

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“…Secondly, in order to obtain electron transfer between the electrode and the redox group of the protein, the distance between them should not be much greater than 14 Å , the maximum observed for electron transfer between two redox centers in proteins [3]. To overcome these challenges, a wide variety of methods using covalent, electrostatic or hydrophobic interactions on numerous electrode materials, including gold, silver, indium oxide and pyrolitic graphite, have been investigated [4].…”

Section: Introductionmentioning

confidence: 99%

Evidence for heme release in layer-by-layer assemblies of myoglobin and polystyrenesulfonate on pyrolitic graphite

2007

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Layer-by-layer assemblies of myoglobin and polystyrenesulfonate (PSS) on pyrolitic graphite have been investigated with the goal of determining the origin of the voltammetric response of these films. From the similar midpoint potential, coverage and electron transfer behavior compared with those of adsorbed free heme, it was concluded that the observed voltammetric peak is due to heme adsorbed at the electrode surface. This suggests that the interactions between the pyrolitic graphite electrode, PSS and myoglobin can result in heme release from the protein followed by heme adsorption on the electrode.

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Recent developments in faradaic bioelectrochemistry

Cited by 473 publications

References 150 publications

Direct Electrochemistry of Porcine Purple Acid Phosphatase (Uteroferrin)

Direct Electrochemistry of Porcine Purple Acid Phosphatase (Uteroferrin)

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

Evidence for heme release in layer-by-layer assemblies of myoglobin and polystyrenesulfonate on pyrolitic graphite

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