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ATP regulates the activity of an alternative oxidase in Trypanosoma brucei
Author(s) -
LuévanoMartínez Luis Alberto,
Girard Richard M. B. M.,
Alencar Mayke Bezerra,
Silber Ariel Mariano
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13790
Subject(s) - alternative oxidase , atp synthase , trypanosoma brucei , chemiosmosis , biochemistry , enzyme , mitochondrion , dihydroxyacetone phosphate , dehydrogenase , oxidase test , chemistry , biology , gene
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 F 1 F o ‐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.