TY - GEN A1 - Yarman, Aysu A1 - Peng, Lei A1 - Wu, Yunhua A1 - Bandodkar, Amay A1 - Gajovic-Eichelmann, Nenad A1 - Wollenberger, Ulla A1 - Hofrichter, Martin A1 - Ullrich, René A1 - Scheibner, Katrin A1 - Scheller, Frieder W. T1 - Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors T2 - Bioanalytical Reviews N2 - Aromatic peroxygenase (APO) from the basidiomycetous mushroom Agrocybe aegerita (AaeAPO) and microperoxidases (MPs) obtained from cytochrome c exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of cytochrome P450 (P450), making MPs and APOs to alternate recognition elements in biosensors for the detection of typical P450 substrates. Here, we discuss recently developed approaches using microperoxidases and peroxygenases in view of their potential to supplement P450 enzymes as recognition elements in biosensors for aromatic compounds. Starting as early as the 1970s, the direct electron transfer between electrodes and the heme group of heme peptides called microperoxidases has been used as a model of oxidoreductases. These MP-modified electrodes are used as hydrogen peroxide detectors based on the catalytic current generated by electrically contacted microperoxidase molecules. A similar catalytic reaction has been obtained for the electrode-immobilised heme protein AaeAPO. However, up to now, no MP-based sensors for substrates have been described. In this review, we present biosensors which indicate 4-nitrophenol, aniline, naphthalene and p-aminophenol based on the peroxide-dependent substrate conversion by electrode-immobilised MP and AaeAPO. In these enzyme electrodes, the signal is generated by the conversion of all substrates, thus representing in complex media an overall parameter. The performance of these sensors and their further development are discussed in comparison with P450-based electrodes. KW - Cytochrome P450 KW - Aromatic peroxygenase KW - Microperoxidase KW - Biosensors Y1 - 2011 UR - http://link.springer.com/article/10.1007%2Fs12566-011-0023-4 U6 - https://doi.org/10.1007/s12566-011-0023-4 SN - 1867-2094 VL - 3 IS - 2-4 SP - 67 EP - 94 ER - TY - GEN A1 - Yarman, Aysu A1 - Gröbe, Glenn A1 - Neumann, Bettina A1 - Kinne, Mathias A1 - Gajovic-Eichelmann, Nenad A1 - Wollenberger, Ulla A1 - Hofrichter, Martin A1 - Ullrich, René A1 - Scheibner, Katrin A1 - Scheller, Frieder W. T1 - The aromatic peroxygenase from Marasmius rutola—a new enzyme for biosensor applications T2 - Analytical and Bioanalytical Chemistry N2 - 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. KW - Unspecific peroxygenase KW - Biosensors KW - Cytochrome P450 KW - Phenolic substances Y1 - 2012 UR - http://link.springer.com/article/10.1007%2Fs00216-011-5497-y U6 - https://doi.org/10.1007/s00216-011-5497-y SN - 1618-2650 VL - 402 IS - 1 SP - 405 EP - 412 ER -