Medical College of Wisconsin
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Spin trapping of the azidyl radical in azide/catalase/H2O2 and various azide/peroxidase/H2O2 peroxidizing systems. J Biol Chem 1985 Apr 10;260(7):4003-6

Date

04/10/1985

Pubmed ID

2984193

Scopus ID

2-s2.0-0021954649 (requires institutional sign-in at Scopus site)   107 Citations

Abstract

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.

Author List

Kalyanaraman B, Janzen EG, Mason RP

Author

Balaraman Kalyanaraman PhD Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Azides
Catalase
Chloride Peroxidase
Electron Spin Resonance Spectroscopy
Horseradish Peroxidase
Hydrogen Peroxide
Lactoperoxidase
Models, Chemical
Oxygen Consumption
Peroxidase
Peroxidases
Sodium Azide