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Differences in mitochondrial NADH dehydrogenase activities in trypanosomatids
P. Čermáková, A. Maďarová, P. Baráth, J. Bellová, V. Yurchenko, A. Horváth
Language English Country Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
PubMed Central
from 2020
ProQuest Central
from 2001-01-01 to 1 year ago
Health & Medicine (ProQuest)
from 2001-01-01 to 1 year ago
Public Health Database (ProQuest)
from 2001-01-01 to 1 year ago
ROAD: Directory of Open Access Scholarly Resources
from 1908
- MeSH
- Species Specificity MeSH
- Mitochondrial Proteins genetics metabolism MeSH
- NADH Dehydrogenase genetics metabolism MeSH
- Protozoan Proteins genetics metabolism MeSH
- Trypanosomatina enzymology genetics MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Complex I (NADH dehydrogenase) is the first enzyme in the respiratory chain. It catalyses the electron transfer from NADH to ubiquinone that is associated with proton pumping out of the matrix. In this study, we characterized NADH dehydrogenase activity in seven monoxenous trypanosomatid species: Blechomonas ayalai, Herpetomonas tarakana, Kentomonas sorsogonicus, Leptomonas seymouri, Novymonas esmeraldas, Sergeia podlipaevi and Wallacemonas raviniae. We also investigated the subunit composition of the complex I in dixenous Phytomonas serpens, in which its presence and activity have been previously documented. In addition to P. serpens, the complex I is functionally active in N. esmeraldas and S. podlipaevi. We also identified 24-32 subunits of the complex I in individual species by using mass spectrometry. Among them, for the first time, we recognized several proteins of the mitochondrial DNA origin.
Department of Biochemistry Faculty of Natural Sciences Comenius University Bratislava Slovakia
Faculty of Science Life Science Research Centre University of Ostrava Ostrava Czech Republic
Institute of Chemistry Slovak Academy of Sciences Bratislava Slovakia
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