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.
Highlights
The azidyl radicalis formed during the oxidation of tem using the spin-trapping ESR technique
Azideis used routinelyas an inhibitor of azide (Fisher) “N-labeled sodium azide (Stohler Isotope Chemicals), myeloperoxidaseand catalase, someconsideration should begiven to the biochemical consequences of formation of the highlyreactive azidyl radical by the peroxidase activity of these enzymes
Oneelectron oxidation of azide to the azidyl radical has been detected by spin trapping in chemical [14,15], photochemical [15,16,17,18,19], electrochemical [15, 20], and radiochemical [17] oxidizing systems
Summary
4003-4006 1985 Printed in C?..S.A. Spin Trapping of the Azidyl Radical in Azide/Catalase/H202and Various Azide/Peroxidase/H202 PeroxidizingSystems*. The azidyl radicalis formed during the oxidation of tem using the spin-trapping ESR technique. The oxidasodium azide by the catalasefiydrogen peroxide sys- tion of azide by horseradish peroxidase, chloroperoxidase, tem, as detected by the ESR spin-trapping technique. Azideis used routinelyas an inhibitor of azide (Fisher) “N-labeled sodium azide (Stohler Isotope Chemicals), myeloperoxidaseand catalase, someconsideration should begiven to the biochemical consequences of formation of the highlyreactive azidyl radical by the peroxidase activity of these enzymes. In addition to inhibiting the catalytic reduction of hydrogen peroxide to water by catalase [1,2], the azide anion concomitantly undergoes extensive oxidation to several gaseous niroom temperature for several hours [26];the HRP was used soon after boiling.
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