Alternative oxidase present in procyclic Trypanosoma brucei may act to lower the mitochondrial production of superoxide

Archives of Biochemistry and Biophysics
Jing Fang, Diana S Beattie

Abstract

The mitochondrial electron transfer chain present in the procyclic form of the African trypanosome Trypanosoma brucei contains both cytochrome c oxidase and an alternative oxidase (TAO) as terminal oxidases that reduce oxygen to water. By contrast, the electron transfer chain of the primitive mitochondrion present in the bloodstream form of T. brucei contains only TAO as the terminal oxidase. TAO functions in the bloodstream forms to oxidize the ubiquinol produced by the glycerol-3-phosphate shuttle that results in the oxidation of the reduced nicotinamide adenine dinucleotide phosphate produced by glycolysis. The function, however, of TAO in the procyclic forms is unknown. In this study, we found that inhibition of TAO by the specific inhibitor salicylhydroxamic acid stimulates the formation of reactive oxygen species (ROS) in trypanosome mitochondria, resulting in mitochondrial alteration and increased oxidation of cellular proteins. Moreover, the activity and protein content of TAO in procyclic trypanosomes were increased when cells were incubated in the presence of hydrogen peroxide or antimycin A, the cytochrome bc1 complex inhibitor, which also results in increased ROS production. We suggest that one function of TAO in pr...Continue Reading

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African trypanosomiasis, also known as sleeping sickness, is an insect-borne parasitic disease of humans and other animals. It is caused by protozoa of the species Trypanosoma brucei and almost invariably progresses to death unless treated. Discover the latest research on African trypanosomiasis here.