Journal
FEBS LETTERS
Volume 594, Issue 13, Pages 2150-2158Publisher
WILEY
DOI: 10.1002/1873-3468.13790
Keywords
alternative oxidase; glycolysis; mitochondria; Trypanosoma brucei
Funding
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [2016/12999-0, 2016/06034-2]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [308351/2013-4, 404769/2018-7]
- Research Council United Kingdom Global Challenges Research Fund under grant agreement 'A Global Network for Neglected Tropical Diseases' [MR/P027989/1]
- MRC [MR/P027989/1] Funding Source: UKRI
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [16/12999-0] Funding Source: FAPESP
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The reduced mitochondrial respiratory chain from the bloodstream forms of Trypanosoma brucei is composed of only a membrane-bound glycerol-3-phosphate dehydrogenase and an alternative oxidase. Since these enzymes are not proton pumps, their functions are restricted to the maintenance of the redox balance in the glycosome by means of the dihydroxyacetone phosphate/glycerol-3-phosphate shuttle. Additionally, an F1Fo-ATP synthase functions as an ATP-hydrolysing enzyme to establish the proton motive force necessary to maintain the basic functions of mitochondria. In this report, we studied the interplay between the alternative oxidase and ATP synthase, and we found that, in addition to its role as a proton pump, ATP synthase contributes to maintain safe levels of ATP to prevent the inhibition of the alternative oxidase by ATP.
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