2020, Ingenbosch, Kim N., Quint, Stephan, Dyllick-Brenzinger, Melanie, Wunschik, Dennis S., Kiebist, Jan, Süss, Philipp, Liebelt, Ute, Zuhse, Ralf, Menyes, Ulf, Scheibner, Katrin, Mayer, Christian, Opwis, Klaus, Gutmann, Jochen S., Hoffmann-Jacobsen, Kerstin

Singlet oxygen is a reactive oxygen species undesired in living cells but a rare and valuable reagent in chemical synthesis. We present a fluorescence spectroscopic analysis of the singlet-oxygen formation activity of commercial peroxidases and novel peroxygenases. Singlet-oxygen sensor green (SOSG) is used as fluorogenic singlet oxygen trap. Establishing a kinetic model for the reaction cascade to the fluorescent SOSG endoperoxide permits a kinetic analysis of enzymatic singlet-oxygen formation. All peroxidases and peroxygenases show singlet-oxygen formation. No singlet oxygen activity could be found for any catalase under investigation. Substrate inhibition is observed for all reactive enzymes. The commercial dye-decolorizing peroxidase industrially used for dairy bleaching shows the highest singlet-oxygen activity and the lowest inhibition. This enzyme was immobilized on a textile carrier and successfully applied for a chemical synthesis. Here, ascaridole was synthesized via enzymatically produced singlet oxygen. © 2020 Wiley-VCH GmbH