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Analytical and Bioanalytical Chemistry

, Volume 402, Issue 1, pp 405–412 | Cite as

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

  • Aysu Yarman
  • Glenn Gröbe
  • Bettina Neumann
  • Mathias Kinne
  • Nenad Gajovic-Eichelmann
  • Ulla Wollenberger
  • Martin Hofrichter
  • René Ullrich
  • Katrin Scheibner
  • Frieder W. Scheller
Original Paper

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.

Keywords

Unspecific peroxygenase Cytochrome P450 Biosensors Phenolic substances 

Notes

Acknowledgments

The authors gratefully acknowledge the financial support of BMBF (0311993) of Germany. This work is a part of UniCat, the Cluster of Excellence in the field of catalysis coordinated by TU Berlin and financially supported by Deutsche Forschungsgemeinschaft within the framework of the German Excellence Initiative (EXC 314).

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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Aysu Yarman
    • 1
  • Glenn Gröbe
    • 2
  • Bettina Neumann
    • 1
  • Mathias Kinne
    • 3
  • Nenad Gajovic-Eichelmann
    • 1
  • Ulla Wollenberger
    • 4
  • Martin Hofrichter
    • 3
  • René Ullrich
    • 3
  • Katrin Scheibner
    • 2
  • Frieder W. Scheller
    • 1
    • 4
  1. 1.Fraunhofer Institute for Biomedical Engineering IBMTPotsdamGermany
  2. 2.Department of BiotechnologyLausitz University of Applied SciencesSenftenbergGermany
  3. 3.Unit of Environmental BiotechnologyInternational Graduate School of ZittauZittauGermany
  4. 4.Institute of Biochemistry and BiologyUniversity of Potsdam Karl-Liebknecht-Str. 24–25GolmGermany

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