The aromatic peroxygenase from Marasmius rutola - a new enzyme for biosensor applications
| Autor: | Martin Hofrichter, Nenad Gajovic-Eichelmann, Bettina Neumann, René Ullrich, Aysu Yarman, Mathias Kinne, Ursula Wollenberger, Frieder W. Scheller, Katrin Scheibner, Glenn Gröbe |
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| Přispěvatelé: | Publica |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Catechol
Hydroquinone Substrate (chemistry) Biosensing Techniques Enzymes Immobilized Biochemistry Combinatorial chemistry Redox Marasmius Analytical Chemistry Mixed Function Oxygenases Substrate Specificity Fungal Proteins chemistry.chemical_compound Aniline chemistry Unspecific peroxygenase Organic chemistry Hydrogen peroxide Biosensor Institut für Biochemie und Biologie |
| Popis: | 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 Fe(2+)/Fe(3+) 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. |
| Databáze: | OpenAIRE |
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