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Singlet‐Oxygen Generation by Peroxidases and Peroxygenases for Chemoenzymatic Synthesis
Author(s) -
Ingenbosch Kim N.,
Quint Stephan,
DyllickBrenzinger Melanie,
Wunschik Dennis S.,
Kiebist Jan,
Süss Philipp,
Liebelt Ute,
Zuhse Ralf,
Menyes Ulf,
Scheibner Katrin,
Mayer Christian,
Opwis Klaus,
Gutmann Jochen S.,
HoffmannJacobsen Kerstin
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000326
Subject(s) - singlet oxygen , chemistry , photochemistry , reagent , catalase , peroxidase , oxygen , substrate (aquarium) , reactive oxygen species , singlet state , fluorescence , enzyme , organic chemistry , excited state , biochemistry , oceanography , physics , quantum mechanics , nuclear physics , geology
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.