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Literature summary for 1.11.2.1 extracted from
- The aromatic peroxygenase from Marasmius rutola - a new enzyme for biosensor applications (2012), Anal. Bioanal. Chem., 402, 405-412.
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | use of enzyme for biosensor applications. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. After immobilization at a chitosan-capped gold-nanoparticle modified glassy carbon electrode, enzyme displays a pair of redox peaks with a midpoint potential of -278.5 mV vs. AgCl/AgCl at 1 M KCl for the Fe2+/Fe3+ redox couple of the heme-thiolate-containing protein. The signal is generated by the reduction of electrode-active reaction products e.g., p-benzoquinone and p-quinoneimine with electroenzymatic recycling of the analyte | Marasmius rotula |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Marasmius rotula | - |
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Release 2023.1 (January 2023)
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