Work

Spin trapping of the azidyl radical in azide/catalase/H2O2 and various azide/peroxidase/H2O2 peroxidizing systems.

Year: 1985

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)89222-5

Authors: B Kalyanaraman, E G Janzen, R P Mason

Institutions: National Institutes of Health, Medical College of Wisconsin, National Institute of Environmental Health Sciences, University of Guelph

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1516090436

FWCI: 1.665

Cites: 36

Cited by: 118

Related to: 10