Singlet oxygen production from the peroxidase-catalyzed oxidation of indole-3-acetic acid.
The aerobic oxidation of indole-3-acetic acid catalyzed by horseradish peroxidase produces 1268 nm emission characteristic of singlet oxygen. Lactoperoxidase also oxidizes indole-3-acetic acid to produce singlet oxygen, but in contrast to horseradish peroxidase, this enzyme system requires hydrogen peroxide. In both of these systems, the intensity of the 1268 nm emission is small due to quenching of the singlet oxygen by indole-3-acetic acid and by reaction products derived from indole-3-acetic acid. The biomolecular reaction of peroxyl radicals via a Russell mechanism is a plausible mechanism for the singlet oxygen generation in these systems. Under typical conditions of p2H 4.0, 1 microM horseradish peroxidase, 1 mM indole-3-acetic acid, and 240 microM oxygen, the singlet oxygen yield was 15 +/- 1 microM or 13% of the amount predicted by the Russell mechanism.
Kanofsky
J R
JR
Medical Service, Edward Hines, Jr., Veterans Administration Hospital, Hines, Illinois 60141.
D006735:Horseradish Peroxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007210:Indoleacetic Acids / Q000378:metabolism*; D007700:Kinetics; D007784:Lactoperoxidase / Q000378:metabolism*; D008163:Luminescent Measurements; D010084:Oxidation-Reduction; D010100:Oxygen; D010544:Peroxidases / Q000378:metabolism*; D010777:Photochemistry; D011190:Potassium Cyanide / Q000494:pharmacology; D026082:Singlet Oxygen
D007210:Indoleacetic Acids; D026082:Singlet Oxygen; C030737:indoleacetic acid; D006735:Horseradish Peroxidase; D007784:Lactoperoxidase; D010544:Peroxidases; D011190:Potassium Cyanide; D010100:Oxygen