Steady-state oxygen kinetics of terminal oxidases in Trypanosoma mega.
Steady-state oxygen kinetics of Trypanosoma mega reveal the presence of 3 oxidases. These include an oxidase which is sensitive to salicylhydroxamic acid (SHAM) but insensitive to sodium azide. This oxidase could be the L-alpha glycerophosphate oxidase present in bloodstream trypanosomes. In addition, and oxidase is present wthich is azide-sensitive but SHAM-insensitive. This oxidase is inhibited by CO and is probably cytochrome aa3. A 3rd oxidase is insensitive to both azide and SHAM but is inhibited by CO and is possibly cytochrome o. Reciprocal plots of T. mega reveal the presence of 2 oxidases that are inhibited by CO. These results are discussed in the light of previous evidence suggesting the presence of several oxidases and a branched electron transport system in T. mega.
D000818:Animals; D001386:Azides / Q000494:pharmacology; D006877:Hydroxamic Acids / Q000494:pharmacology; D007700:Kinetics; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010101:Oxygen Consumption; D012457:Salicylamides / Q000494:pharmacology; D014345:Trypanosoma / Q000201:enzymology*
D001386:Azides; D006877:Hydroxamic Acids; D012457:Salicylamides; C005703:salicylhydroxamic acid; D010088:Oxidoreductases