@misc{IngenboschQuintDyllickBrenzingeretal., author = {Ingenbosch, Kim N. and Quint, Stephan and Dyllick-Brenzinger, Melanie and Wunschik, Dennis S. and Kiebist, Jan and S{\"u}ss, Philipp and Liebelt, Ute and Zuhse, Ralf and Menyes, Ulf and Scheibner, Katrin and Mayer, Christian and Opwis, Klaus and Gutmann, Jochen S. and Hoffmann-Jacobsen, Kerstin}, title = {Singlet oxygen generation by peroxidases and peroxygenases for chemo-enzymatic synthesis}, series = {ChemBioChem}, volume = {22}, journal = {ChemBioChem}, number = {2}, issn = {1439-7633}, doi = {10.1002/cbic.202000326}, pages = {398 -- 407}, abstract = {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.}, language = {en} }