Hydrogen peroxide and .beta.-nicotinamide adenine dinucleotide sensing amperometric electrodes based on electrical connection of horseradish peroxidase redox centers to electrodes through a three-dimensional electron relaying polymer network

Vreeke, Mark; Maidan, Ruben; Heller, Adam

doi:10.1021/ac00048a004

Cited by 220 publications

(115 citation statements)

References 22 publications

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“…The latter remains the most common form of biosensor despite requiring a large overpotential at which reducing agents present in the sample can contribute to the faradaic current. Although some of the problems associated with anodic H 2 O 2 detection have been minimized by using electrocatalytic H 2 O 2 reduction at low potentials (Gao et al, 1992;Vreeke et al, 1992;Wang et al, 1994Wang et al, , 1996, the question of sensitivity to pO 2 appears in an additional form */the possibility of direct faradaic reduction of O 2 .…”

Section: Introductionmentioning

confidence: 99%

Characterization in vitro and in vivo of the oxygen dependence of an enzyme/polymer biosensor for monitoring brain glucose

Dixon

Lowry

O’Neill

2002

Journal of Neuroscience Methods

108

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The oxygen dependence of a first generation amperometric biosensor was investigated in vitro and in vivo by monitoring its glucose response as a function of solution pO 2 . The biosensor was a glucose oxidase (GOx) modified poly(o -phenylenediamine) coated Pt cylinder electrode (Pt/PPD/GOx) that has been designed for neurochemical analysis in vivo. Two types of oxygen probes were used: a self-calibrating commercial macroelectrode in vitro; and a carbon paste microelectrode in vivo. Calibrations in vitro showed that oxygen interference in the operation of Pt/PPD/GOx electrodes was minimal for concentrations of glucose ( Â/0.5 mM) and oxygen ( Â/50 mM) found in brain ECF. This observation was confirmed by simultaneous monitoring in vivo of brain glucose and oxygen in the awake rat. However, at levels of glucose normally found in peripheral tissues ( Â/5 mM), the oxygen dependence was severe. We conclude that the oxygen sensitivity of Pt/PPD/GOx biosensors does not preclude their reliable use in media containing low glucose levels, such as brain ECF. #

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Section: Introductionmentioning

confidence: 99%

Characterization in vitro and in vivo of the oxygen dependence of an enzyme/polymer biosensor for monitoring brain glucose

Dixon

Lowry

O’Neill

2002

Journal of Neuroscience Methods

108

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“…It was polished down to 0.3 μM with Al 2 O 3 slurry and then sonicated in an ultrasonic water bath with ethanol, acetone and deioinzed water, respectively. Peroxdidase redox polymer (PRP), which has been shown to be highly sensitive for H 2 O 2 detection [15] was then immobilized on the dual gold electrode and the resultant electrode was assembled onto the cell that also contained a platinum wire auxiliary electrode and an Ag/AgCl reference electrode. The PRP-modified electrode was fabricated by coating 2 μL of PRP on the gold dual electrodes and stored in a vacuum dessicator overnight to dry.…”

Section: Isolation Of Arabidopsis Chloroplastsmentioning

confidence: 99%

“…Thus, either the endogenous H 2 O 2 in the extracts already reacted prior to our experiments or, more likely, the levels were below 0.5 mM. We thus used amperommetry using an electrode coated with horseradish peroxidase to amplify the H 2 O 2 signal [15]. The data are presented in Fig.…”

Section: Activation Of Chloroplast Lox Activity By Hydrogen Peroxidementioning

confidence: 99%

The developmental transition to flowering in Arabidopsis is associated with an increase in leaf chloroplastic lipoxygenase activity

Bañuelos¹,

Argumedo²,

Patel³

et al. 2008

Plant Science

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The developmental transition from vegetative growth to flowering in Arabidopsis is associated with a precipitous decline in the activity of leaf ascorbate peroxidase (APx), an enzymatic scavenger of hydrogen peroxide, and an increase in specific lipid peroxidation leading to the accumulation of 13-hydroperoxy-9,11,15 (Z,E,Z) octadecatrienoic acid (13 HOO-FA). The appearance of this specific isomer suggests that it is of enzymatic origin and may represent the activation of an oxylipin signaling pathway. We thus hypothesized that leaf 13-lipoxygenase (LOX) activity increases at the floral transition and leads to the observed elevation of 13-HOO-FA levels. Leaf protein extracts were prepared from seven distinct life stages of Arabidopsis plants and used to assay for LOX activity. We report that leaf 13-LOX enzymatic activity increases twoto three-fold from the vegetative stage to the immediate post-floral transition stage. We found two forms of LOX activity in cell extracts and show that the higher pH optimum form is the isoenzyme activated. This increase is correlated with a small increase in H 2 O 2 , perhaps resulting from the previously reported decline in leaf APx activity. Very low levels of exogenous H 2 O 2 activate the induced form in vegetative leaf extracts in vitro, suggesting that the floral transition-dependent APx decline and subsequent H 2 O 2 elevation are involved in activating plastid 13-LOX and thus a second messenger oxylipin pathway.

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“…Os-polyvinylpyridine containing horseradish peroxidase (Os-gel-HRP) was obtained from Bioanalytical Systems Inc. (West Lafayette, IN). 37,38 Glutamate oxidase (GluOx) from streptomyces sp. X-119-6 was obtained from Yamasa Shoyu (Choshi, Japan).…”

Section: Chemicals and Materialsmentioning

confidence: 99%

Microfabricated On-Line Sensor for Continuous Monitoring of l-Glutamate

Niwa

Horiuchi

Kurita³

et al. 1998

ANAL. SCI.

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Various methods have been developed for measuring the in vivo and in vitro concentrations of L-glutamate, since glutamate plays an important role in synaptic efficacy, including the long-term potentiation (LTP) 1,2 and long-term depression (LTD) 3,4 of excitatory neurotransmission. It is also reported to be a factor in several diseases including ischemia and nerve cell death.5,6 A number of methods have already been proposed for measuring L-glutamate, including chromatographic technique 7 and capillary electrophoresis. 8,9 However, these methods require time for derivatization and column separation.Recently, many groups have been focusing on the development of amperometric enzyme sensors using glutamate dehydrogenase and glutamate oxidase. The latter enzyme has more often been used to fabricate glutamate sensors because a glutamate dehydrogenase sensor requires the addition of NAD + . 10-12 Therefore, glutamate oxidase has been more often used to fabricate electrochemical sensors for detecting the neurotransmitter, L-glutamate. [13][14][15][16][17][18][19][20][21][22][23][24] Carbon fiber or metal wire microelectrodes modified with glutamate oxidase have been employed for measuring L-glutamate in the brain and in cultured rat brain tissue. [13][14][15][16] It has been reported that L-glutamate increases as the result of KCl and electrical stimulations. The advantages of the enzyme-modifed electrodes are their fast response and their ability to measure a small localized area.By contrast, on-line L-glutamate sensors have been developed. These consist of a syringe pump, a microdialysis (MD) sampling probe, an enzymatic reactor and an electrode in a flow cell. [17][18][19][20][21][22] On-line sensors are particularly useful for measuring in vivo L-glutamate, since they are very stable. This is because the flow measurement is very reproducibile and the MD membrane eliminates high molecular weight interferents such as proteins. The reported detection limits of online L-glutamate sensors are from 10 nM to 0.5 µM, which are lower than those of microelectrode-based sensors. However, the on-line sensor response is slower than that of the microelectrode sensors and it has a large sampling probe (usually 1 -3 mm long and a few hundred µm in diameter). There have been a few reports on the use of on-line sensors for measuring cultured nerve cells. However, their slow response and large sampling probe size limits their spatial and temporal resolutions in spite of their high sensitivity and long term stability. 21,22 We reported an on-line L-glutamate sensor for measuring dissociated nerve cell cultures. 23 The sensor consists of a glass capillary for sampling combined with an electrochemical thin layer flow cell. Since the sampling probe is much smaller than the MD probe, we can achieve better spatial resolution. We observed the transient release of L-glutamate by stimulating the inhibitory neurotransmitter, γ-aminobutyric acid (GABA), using this sensor. 24 However, the relatively large volume of the sensor means that there ...

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Hydrogen peroxide and .beta.-nicotinamide adenine dinucleotide sensing amperometric electrodes based on electrical connection of horseradish peroxidase redox centers to electrodes through a three-dimensional electron relaying polymer network

Cited by 220 publications

References 22 publications

Characterization in vitro and in vivo of the oxygen dependence of an enzyme/polymer biosensor for monitoring brain glucose

Characterization in vitro and in vivo of the oxygen dependence of an enzyme/polymer biosensor for monitoring brain glucose

The developmental transition to flowering in Arabidopsis is associated with an increase in leaf chloroplastic lipoxygenase activity

Microfabricated On-Line Sensor for Continuous Monitoring of l-Glutamate

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