Spin trapping of the azidyl radical in azide/catalase/H2O2 and various azide/peroxidase/H2O2 peroxidizing systems.
The azidyl radical is formed during the oxidation of sodium azide by the catalase/hydrogen peroxide system, as detected by the ESR spin-trapping technique. The oxidation of azide by horseradish peroxidase, chloroperoxidase, lactoperoxidase, and myeloperoxidase also forms azidyl radical. It is suggested that the evolution of nitrogen gas and nitrogen oxides reported in the azide/catalase/hydrogen peroxide system results from reactions of the azidyl radical. The azide/horseradish peroxidase/hydrogen peroxide system consumes oxygen, and this oxygen uptake is inhibited by the spin trap 5,5-dimethyl-1-pyrroline-N-oxide, presumably due to the competition with oxygen for the azidyl radical. Although azide is used routinely as an inhibitor of myeloperoxidase and catalase, some consideration should be given to the biochemical consequences of the formation of the highly reactive azidyl radical by the peroxidase activity of these enzymes.
Kalyanaraman
B
B
Janzen
E G
EG
Mason
R P
RP
D001386:Azides / Q000378:metabolism*; D002374:Catalase / Q000378:metabolism*; D002711:Chloride Peroxidase / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D006735:Horseradish Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D007784:Lactoperoxidase / Q000378:metabolism; D008956:Models, Chemical; D010101:Oxygen Consumption; D009195:Peroxidase / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism*; D019810:Sodium Azide
D001386:Azides; D019810:Sodium Azide; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D007784:Lactoperoxidase; D010544:Peroxidases; D002711:Chloride Peroxidase; D002374:Catalase; D009195:Peroxidase