Peroxidatic degradation of azide by catalase and irreversible enzyme inactivation.
A study of the azide reaction with bovine liver catalase in presence of hydrogen peroxide has been performed, using conventional UV-visible spectrometry and activity measurements. Compound III and NO-ferrocatalase were the predominant forms of the enzyme observed in air and under nitrogen, respectively. A reaction scheme for peroxidatic degradation of azide by catalase is proposed. Accordingly, accumulation of Compound III is the main factor responsible for the reversible inhibition of 'catalatic' activity by azide, while formation of a complex between native catalase and azide has a negligible effect. Catalase is irreversibly inactivated by prolonged exposure to high levels of H2O2 and azide. The latter involves cleavage of the prosthetic group with liberation of the heme iron. Both in air and under nitrogen, generation of azidyl radicals seems to play a minor role in the irreversible inactivation process.
Lardinois
O M
OM
Unité de Chimie des Interfaces, Université Catholique de Louvain, Louvain-la-Neuve, Belgium. Lardinois@cifa.ucl.ac.be
Rouxhet
P G
PG
D000818:Animals; D001386:Azides / Q000378:metabolism*; D002374:Catalase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002417:Cattle; D004789:Enzyme Activation; D006861:Hydrogen Peroxide / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D013056:Spectrophotometry, Ultraviolet
D001386:Azides; D006861:Hydrogen Peroxide; D002374:Catalase