Singlet oxygen production from the peroxidase catalyzed formation of styrene glutathione adducts.
Recently, Stock et al. (J. Biol. Chem. 261, 15915-15922 [1986]) described a model enzyme system composed of horseradish peroxidase, hydrogen peroxide, phenol, glutathione and styrene. This system forms glutathione-styrene conjugates. Glutathione radicals and carbon-centered radicals are intermediates in this process. In the present study, this model enzyme system was also shown to generate singlet oxygen, probably via a Russell mechanism. No singlet oxygen was generated in the absence of styrene. Thus, contrary to prior suggestions, the reaction of glutathione radical with oxygen to produce a thiyl peroxyl radical is not a significant source of singlet oxygen.
Kanofsky
J R
JR
Medical Service, Edward Hines, Jr., Veterans Administration Hospital, Hines, IL 60141.
D005978:Glutathione / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D008163:Luminescent Measurements; D010100:Oxygen / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010777:Photochemistry; D026082:Singlet Oxygen; D013343:Styrenes / Q000378:metabolism*
D013343:Styrenes; D026082:Singlet Oxygen; D006735:Horseradish Peroxidase; D010544:Peroxidases; D005978:Glutathione; D010100:Oxygen