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The aromatic peroxygenase from <i>Marasmius rutola</i>—a new enzyme for biosensor applications
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The aromatic peroxygenase from Marasmius rutola—a new enzyme for biosensor applications

Author: Aysu Yarman Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, GermanyGlenn Gröbe Affiliation: Department of Biotechnology, Lausitz University of Applied Sciences, Senftenberg, 01968, GermanyBettina Neumann Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, GermanyMathias Kinne Affiliation: Unit of Environmental Biotechnology, International Graduate School of Zittau, Zittau, 0276, GermanyNenad Gajovic-Eichelmann Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, GermanyAll authors
Edition/Format: Article Article : English
Publication:Analytical and Bioanalytical Chemistry, v402 n1 (201201): 405-412
Other Databases: WorldCatWorldCatWorldCat
Summary:
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 sensors and their further development are discussed.  Read more...
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Document Type: Article
All Authors / Contributors: Aysu Yarman Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, Germany; Glenn Gröbe Affiliation: Department of Biotechnology, Lausitz University of Applied Sciences, Senftenberg, 01968, Germany; Bettina Neumann Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, Germany; Mathias Kinne Affiliation: Unit of Environmental Biotechnology, International Graduate School of Zittau, Zittau, 0276, Germany; Nenad Gajovic-Eichelmann Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, Germany; Ulla Wollenberger Affiliation: Institute of Biochemistry and Biology, University of Potsdam Karl-Liebknecht-Str. 24-25, Golm, 14476, Germany; Martin Hofrichter Affiliation: Unit of Environmental Biotechnology, International Graduate School of Zittau, Zittau, 0276, Germany; René Ullrich Affiliation: Unit of Environmental Biotechnology, International Graduate School of Zittau, Zittau, 0276, Germany; Katrin Scheibner Affiliation: Department of Biotechnology, Lausitz University of Applied Sciences, Senftenberg, 01968, Germany; Frieder W Scheller Affiliation: Fraunhofer Institute for Biomedical Engineering IBMT, Potsdam, 14476, Germany, +49-331-9775123, +49-331-9775050
ISSN:1618-2642
Language Note: English
Unique Identifier: 5659063863
Notes: Published in the 10th Anniversary Issue.
Aysu Yarman and Glenn Gröbe contributed equally to this work.
Awards:

Abstract:

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 sensors and their further development are discussed.

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