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The aromatic peroxygenase from Marasmius rutola—a new enzyme for biosensor applications

  • The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of −278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe2+/Fe3+ redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensorsThe aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of −278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe2+/Fe3+ redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.show moreshow less

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Author: Aysu Yarman, Glenn Gröbe, Bettina Neumann, Mathias Kinne, Nenad Gajovic-Eichelmann, Ulla Wollenberger, Martin HofrichterORCiD, René UllrichORCiD, Katrin Scheibner, Frieder W. Scheller
URL:http://link.springer.com/article/10.1007%2Fs00216-011-5497-y
DOI:https://doi.org/10.1007/s00216-011-5497-y
ISSN:1618-2650
Title of the source (English):Analytical and Bioanalytical Chemistry
Document Type:Scientific journal article peer-reviewed
Language:English
Year of publication:2012
Tag:Biosensors; Cytochrome P450; Phenolic substances; Unspecific peroxygenase
Volume/Year:402
Issue number:1
First Page:405
Last Page:412
Faculty/Chair:Fakultät 2 Umwelt und Naturwissenschaften / FG Enzymtechnologie
Institution name at the time of publication:Fakultät für Naturwissenschaften (eHL) / Prof. Enzymtechnologie
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