Comparison of Enzymatic Recycling Electrodes for Measuring Aminophenol: Development of a Highly Sensitive Natriuretic Peptide Assay System

Mie, Yasuhiro; Kowata, Keiko; Hirano, Yu; Niwa, Osamu; Mizutani, Fumio

doi:10.2116/analsci.24.577

Cited by 9 publications

(6 citation statements)

References 32 publications

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“…The catalytic activity of microperoxidases is sufficient at 10 µm peroxide for the signal generation/oxidation of HRP substrates, e.g., pAP, catechols or ascorbic acid, but also the hydroxylation of aniline and dehalogenation of 4-fluoroaniline. The lower limit of detection for pAP is almost 70 times lower than for the direct anodic oxidation of pAP [ 45 ] and comparable to previously published papers with different enzyme systems which exploit bi-enzymatic or electro-enzymatic signal amplification [ 46 , 47 , 48 , 49 ].…”

Section: Resultssupporting

confidence: 82%

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

et al. 2012

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In view of the role ascribed to the peroxidatic activity of degradation products of cytochrome c (cyt c) in the processes of apoptosis, we investigate the catalytic potential of heme and of the cyt c derived heme peptide MP-11 to catalyse the cathodic reduction of hydrogen peroxide and to oxidize aromatic compounds. In order to check whether cyt c has an enzymatic activity in the native state where the protein matrix should suppress the inherent peroxidatic activity of its heme prosthetic group, we applied a biocompatible immobilization matrix and very low concentrations of the co-substrate H2O2. The biocatalysts were entrapped on the surface of a glassy carbon electrode in a biocompatible chitosan layer which contained gold nanoparticles. The electrochemical signal for the peroxide reduction is generated by the redox conversion of the heme group, whilst a reaction product of the substrate oxidation is cathodically reduced in the substrate indication. The catalytic efficiency of microperoxidase-11 is sufficient for sensors indicating HRP substrates, e.g., p-aminophenol, paracetamol and catechol, but also the hydroxylation of aniline and dehalogenation of 4-fluoroaniline. The lower limit of detection for p-aminophenol is comparable to previously published papers with different enzyme systems. The peroxidatic activity of cyt c immobilized in the chitosan layer for catechol was found to be below 1 per mill and for p-aminophenol about 3% as compared with that of heme or MP-11.

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Section: Resultssupporting

confidence: 82%

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

et al. 2012

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“…The limit of detection was determined to be 3.9 nM (S/N=3). This value is in the range of previously published papers with different enzymes [125][126][127][128][129][130].…”

Section: Peroxide-dependent Oxidation Of P-aminophenol and Anilinesupporting

confidence: 65%

Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors

Yarman

Peng

et al. 2011

Bioanal Rev

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Aromatic peroxygenase (APO) from the basidiomycetous mushroom Agrocybe aegerita (AaeAPO) and microperoxidases (MPs) obtained from cytochrome c exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of cytochrome P450 (P450), making MPs and APOs to alternate recognition elements in biosensors for the detection of typical P450 substrates. Here, we discuss recently developed approaches using microperoxidases and peroxygenases in view of their potential to supplement P450 enzymes as recognition elements in biosensors for aromatic compounds. Starting as early as the 1970s, the direct electron transfer between electrodes and the heme group of heme peptides called microperoxidases has been used as a model of oxidoreductases. These MP-modified electrodes are used as hydrogen peroxide detectors based on the catalytic current generated by electrically contacted microperoxidase molecules. A similar catalytic reaction has been obtained for the electrode-immobilised heme protein AaeAPO. However, up to now, no MP-based sensors for substrates have been described. In this review, we present biosensors which indicate 4-nitrophenol, aniline, naphthalene and p-aminophenol based on the peroxide-dependent substrate conversion by electrode-immobilised MP and AaeAPO. In these enzyme electrodes, the signal is generated by the conversion of all substrates, thus representing in complex media an overall parameter. The performance of these sensors and their further development are discussed in comparison with P450-based electrodes

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“…In the field of electrochemical immunosensing using alkaline phosphatase (ALP) as the enzyme label, p-aminophenyl phosphate (p-APP) is commonly used as a substrate of ALP because of the facile electrochemical detection of the enzymatic reaction product, p-aminophenol (p-AP). [1][2][3] A hydrolytic reaction between ALP and p-APP releases p-AP, which is then detected to indicate the number of immunoreactions. However, in detection, calibration of p-AP can be difficult because of the chemical instability of p-AP, which can oxidize in alkaline media in the presence of oxygen.…”

Section: Introductionmentioning

confidence: 99%

Nanomolar detection of p-nitrophenol via in situ generation of p-aminophenol at nanostructured microelectrodes

Boateng

Brajter-Toth

2012

Analyst

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Comparison of Enzymatic Recycling Electrodes for Measuring Aminophenol: Development of a Highly Sensitive Natriuretic Peptide Assay System

Cited by 9 publications

References 32 publications

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors

Nanomolar detection of p-nitrophenol via in situ generation of p-aminophenol at nanostructured microelectrodes

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