Comparison of rotating disk and wall-jet electrode systems for studying the kinetics of direct and mediated electron transfer for horseradish peroxidase on a graphite electrode

Lindgren, Annika; Munteanu, Florentina-Daniela; Gazaryan, I. G.; Ruzgas, Tautgirdas; Gorton, Lo

doi:10.1016/s0022-0728(98)00326-x

Cited by 58 publications

(60 citation statements)

References 24 publications

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“…This is an electrochemical analog of a classical method of steady-state enzyme kinetics. Technically, this experiment can be performed either at a rotating disk electrode [11] or under flow conditions [12]. The developed approach is based on a comparison between direct electron transfer and mediated electron transfer at the same electrode.…”

Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

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Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

et al. 2005

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Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

“…In addition to the fundamental studies of natural glycosylated TOP performed in 1996-1999 [3][4][5][6], which demonstrated a number of practically promising properties of this enzyme, the new enzyme was also tested for analytical purposes [7][8][9][10][11][12][13][14][15][16][17][18][19][20].…”

mentioning

confidence: 99%

Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

et al. 2005

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“…For the HRP-catalyzed reduction of H 2 O 2 (Reaction 4), n = 2. Both the HRP-modified electrodes (36,37) and the Fe-based peroxidase mimetics (20) mentioned above also report n = 2, i.e. H 2 O 2 in these systems is reduced to H 2 O by a Fe-mediated reaction.…”

Section: Ecs Transactionsmentioning

confidence: 95%

Peroxidase Mimetic Activity at Tailored Nanocarbon Electrodes

Lyon

Stevenson²

2009

ECS Trans.

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We demonstrate here the intrinsic reactivity of nitrogen-doped carbon nanotubes (N-CNTs) toward H2O2 consumption and their use as a potential peroxidase mimetic. Analysis of N-CNT-modified glassy carbon electrodes in an rotating disk electrode (RDE) amperometry configuration indicates that the mechanism of H2O2 consumption is not a 2-electron reduction to H2O, as is observed for peroxidase-catalyzed H2O2 reduction. We believe that the N-CNT reaction mechanism toward H2O2 occurs through the decomposition of H2O2 to O2 and H2O, resulting in an increase in current at the N-CNT electrode as the newly generated H2O2 is electrochemically reduced. We have exploited this intrinsic reactivity by incorporating N-CNTs as a substitute for horseradish peroxidase (HRP) in a traditionally bi-enzymatic sensing scheme for the detection of glucose. These studies serve as proof of concept for the use of N-CNTs as a peroxidase mimetic in unmediated biogenic analyte detection.

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“…Peroxidase catalyses the electrochemical reduction of H 2 O 2 produced by GOD through a direct electron transfer reaction at a much lower applied potential compared with electrochemical oxidation of H 2 O 2 and maximum catalytic current can be obtained at carbon electrodes in a potential range of -0.1 and 0 V [2-14]. However, the kinetics of the direct electron transfer from an electrode to the peroxidase is a sluggish process [15][16][17] hence the advantage of using a mediator.The introduction of a mediator in the bienzymatic system (GOD/HRP) leads to an acceleration of the electron transfer, a decrease in the applied working potential (the reduction of the mediator is detected at the electrode) and an increase in sensitivity. The use of mediators is a well-known technique although the way of adding the mediator to the bienzymatic system (oxidase/peroxidase) may vary.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA

Rondeau

Larsson²,

Boujtita

et al. 1999

Analusis

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Amperometric biosensors based on enzymes are interesting due to their high sensitivity, excellent selectivity, simplicity, low cost and rapid response. The most frequently used enzymatic methods for glucose determination employ glucose oxidase (GOD), due to its high selectivity towards ß-D-glucose. In the presence of GOD, the oxidation of glucose occurs, producing H 2 O 2 . Most commonly, the electrochemical detection is performed through the anodic oxidation of H 2 O 2 [1]. A drawback with this detection technique is that high overvoltages are required, and an applied potential in the range of 0.6-1.1 V vs. Ag/AgCl is necessary. Working at such high potentials increases the risk of interference from easily oxidisable compounds such as ascorbate, ureate, acetaminophen, paracetamol, phenols, etc. which are common compounds in biological samples.A possible way of improving the selectivity of such a biosensor is to couple a second enzyme (peroxidase) to the oxidase, creating a bienzymatic sensor. Peroxidase catalyses the electrochemical reduction of H 2 O 2 produced by GOD through a direct electron transfer reaction at a much lower applied potential compared with electrochemical oxidation of H 2 O 2 and maximum catalytic current can be obtained at carbon electrodes in a potential range of -0.1 and 0 V [2-14]. However, the kinetics of the direct electron transfer from an electrode to the peroxidase is a sluggish process [15][16][17] hence the advantage of using a mediator.The introduction of a mediator in the bienzymatic system (GOD/HRP) leads to an acceleration of the electron transfer, a decrease in the applied working potential (the reduction of the mediator is detected at the electrode) and an increase in sensitivity. The use of mediators is a well-known technique although the way of adding the mediator to the bienzymatic system (oxidase/peroxidase) may vary. A number of different mediators have been used as additions into sample solutions such as, potassium hexacyanoferrate (II) [18][19][20][21][22][23][24] [44,45], and Nafion-Nmethyl phenazinium [46]. The advantages of using the redox polymers are several, but mainly they result in more stable biosensors since leaking of the mediator from the electrode is minimised and higher and faster responses are observed due to the proximity between the enzyme and the mediator. Although, choosing an appropriate bulk matrix and mediator concentration these properties can be achieved with nonpolymeric mediators and recently a ferrocene mediated bienzymatic graphite-Teflon electrode has been developed for batch and flow-injection measurements [47]. On the other hand several biosensors based on monoenzymatic electrodes 649The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA Abstract. A bienzymatic biosensor incorporating a mediator has been developed in order to achieve a fast and selective detection of glucose in a flow injection system. The working electrode is based on a carbon paste matrix bulk modified with glucose ...

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Comparison of rotating disk and wall-jet electrode systems for studying the kinetics of direct and mediated electron transfer for horseradish peroxidase on a graphite electrode

Cited by 58 publications

References 24 publications

Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

Peroxidase Mimetic Activity at Tailored Nanocarbon Electrodes

The synergetIc effect of redox mediators and peroxidase in a bienzymatic biosensor for glucose assays in FIA

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