Trichomonas vaginalis: NADH oxidase activity

Tanabe, Masanobu

doi:10.1016/0014-4894(79)90063-8

Cited by 27 publications

(17 citation statements)

References 17 publications

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“…For example, oxygen-reducing NADH oxidases are present in the cytosol of Entamoeba histolytica (289), Giardia lamblia (278), Trichomonas vaginalis (281,356,489), and Tritrichomonas foetus (78,345). Again, we designate eukaryotes that have no requirement for O 2 in their core energy metabolism "anaerobes," using the term anaerobic to indicate that the organisms in question do not require free O 2 for survival and multiplication.…”

Section: Anaerobes and Microaerophiles: Redox Balance With A Pinch Ofmentioning

confidence: 99%

See 1 more Smart Citation

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Müller

Mentel

Hellemond

et al. 2012

Microbiol Mol Biol Rev

687

904

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SUMMARY Major insights into the phylogenetic distribution, biochemistry, and evolutionary significance of organelles involved in ATP synthesis (energy metabolism) in eukaryotes that thrive in anaerobic environments for all or part of their life cycles have accrued in recent years. All known eukaryotic groups possess an organelle of mitochondrial origin, mapping the origin of mitochondria to the eukaryotic common ancestor, and genome sequence data are rapidly accumulating for eukaryotes that possess anaerobic mitochondria, hydrogenosomes, or mitosomes. Here we review the available biochemical data on the enzymes and pathways that eukaryotes use in anaerobic energy metabolism and summarize the metabolic end products that they generate in their anaerobic habitats, focusing on the biochemical roles that their mitochondria play in anaerobic ATP synthesis. We present metabolic maps of compartmentalized energy metabolism for 16 well-studied species. There are currently no enzymes of core anaerobic energy metabolism that are specific to any of the six eukaryotic supergroup lineages; genes present in one supergroup are also found in at least one other supergroup. The gene distribution across lineages thus reflects the presence of anaerobic energy metabolism in the eukaryote common ancestor and differential loss during the specialization of some lineages to oxic niches, just as oxphos capabilities have been differentially lost in specialization to anoxic niches and the parasitic life-style. Some facultative anaerobes have retained both aerobic and anaerobic pathways. Diversified eukaryotic lineages have retained the same enzymes of anaerobic ATP synthesis, in line with geochemical data indicating low environmental oxygen levels while eukaryotes arose and diversified.

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Section: Anaerobes and Microaerophiles: Redox Balance With A Pinch Ofmentioning

confidence: 99%

“…The enzyme from Trichomonas (281,489) and that from Giardia (58, 364) have been characterized. Homologs of the NADH oxidase genes reported for Giardia and Entamoeba (364) are common among eukaryotic genomes.…”

Section: Anaerobes and Microaerophiles: Redox Balance With A Pinch Ofmentioning

confidence: 99%

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Müller

Mentel

Hellemond

et al. 2012

Microbiol Mol Biol Rev

687

904

View full text Add to dashboard Cite

show abstract

“…The assay mixture for measurement of fumarate reductase activity consisted of 100 mM sodium phosphate buffer pH 7n5, 10 mM DTT, 500 mM fumarate and 10 mM NADH. The activity of hydrogenosomal (EC 1;1;1;39) and cytoplasmic (EC 1;1;1;40) malic enzyme was measured aerobically at 340 nm as the rate of NAD + and NADP + reduction, respectively (Drmota et al, 1996), whilst NADH oxidase (EC 1;6;99;3) was determined as the rate of NADH oxidation (Tanabe, 1979).…”

Section: Methodsmentioning

confidence: 99%

Iron-induced changes in pyruvate metabolism of Tritrichomonas foetus and involvement of iron in expression of hydrogenosomal proteins

et al. 2001

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The main function of the hydrogenosome, a typical organelle of trichomonads, is to convert malate or pyruvate to H 2 , CO 2 and acetate by a pathway associated with ATP synthesis. This pathway relies on activity of iron-sulfur proteins such as pyruvate :ferredoxin oxidoreductase (PFOR), hydrogenase and ferredoxin. To examine the effect of iron availability on proper hydrogenosomal function, the metabolic activity of the hydrogenosome and expression of hydrogenosomal enzymes were compared in Tritrichomonas foetus maintained under iron-rich (150 µM iron nitrilotriacetate) or ironrestricted (180 µM 2,2-dipyridyl) conditions in vitro. The activities of PFOR and hydrogenase, and also production of acetate and H 2 , were markedly decreased or absent in iron-restricted trichomonads. Moreover, a decrease in activity of the hydrogenosomal malic enzyme, which is a non-Fe-S protein, was also observed. Impaired function of hydrogenosomes under iron-restricted conditions was compensated for by activation of the cytosolic pathway, mediating conversion of pyruvate to ethanol via acetaldehyde. This metabolic switch was fully reversible. Production of hydrogen by iron-restricted trichomonads was restored to the level of organisms grown under iron-rich conditions within 3 h after addition of 150 µM iron nitrilotriacetate. Protein analysis of purified hydrogenosomes from iron-restricted cells showed decreased levels of proteins corresponding to PFOR, malic enzyme and ferredoxin. Accordingly, these cells displayed decreased steady-state level and synthesis of mRNAs encoding PFOR and hydrogenosomal malic enzyme. These data demonstrate that iron is essential for function of the hydrogenosome, show its involvement in the expression of hydrogenosomal proteins and indicate the presence of iron-dependent control of gene transcription in Tt. foetus.

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“…Due to its anaerobic metabolism, T. vaginalis has to effectively remove intracellular oxygen in order to prevent the deactivation of essential enzymes such as pyruvate:ferredoxin oxidoreductase (PFOR) and hydrogenase (Lloyd and Kristensen, 1985). Two major oxygen scavenging activities have been identified which both reside in the cytoplasm (Tanabe 1979;Linstead and Bradley, 1988): NADPH oxidase and NADH oxidase. The former reduces flavin mononucleotide (FMN) and other flavins through oxidation of NADPH (Linstead and Bradley 1988;Leitsch et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…Reduced FMN, in turn, rapidly reacts with molecular oxygen to form hydrogen peroxide (Chapman et al, 1999;Leitsch et al, 2014). The latter reduces molecular oxygen to water (Tanabe, 1979) by harnessing electrons derived from NADH. The gene for NADPH oxidase, which has been renamed to flavin reductase, was recently identified and characterized (Leitsch et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Identification of the NADH-oxidase gene in Trichomonas vaginalis

Lamien-Meda

Leitsch

2019

Parasitol Res

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The microaerophilic human parasite Trichomonas vaginalis causes infections in the urogenital tract and is one of the most often sexually transmitted pathogens worldwide. Due to its anaerobic metabolism, it has to quickly remove intracellular oxygen in order to avoid deactivation of essential metabolic enzymes such as oxygen-sensitive pyruvate:ferredoxin oxidoreductase (PFOR). Two major enzyme activities which are responsible for the removal, i.e. reduction, of molecular oxygen have been identified in T. vaginalis flavin reductase, formerly designated NADPH oxidase, which indirectly reduces oxygen to hydrogen peroxide via flavin mononucleotide (FMN), and NADH oxidase which reduces oxygen to water. Flavin reductase has been identified and characterized at the gene level as well as enzymatically, but NADH oxidase has so far only been characterized enzymatically with enzyme isolated from T. vaginalis cell extracts. In this study, we identified NADH oxidase by mass spectrometry after isolation of the enzyme from gel bands positively staining for NADH oxidase activity. In strain C1 (ATCC 30001) which is known to lack NADH oxidase activity completely, the NADH oxidase gene has a deletion at position 1540 of the open reading frame leading to a frame shift and, as a consequence, to premature termination of the encoded polypeptide.

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Trichomonas vaginalis: NADH oxidase activity

Cited by 27 publications

References 17 publications

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Iron-induced changes in pyruvate metabolism of Tritrichomonas foetus and involvement of iron in expression of hydrogenosomal proteins

Identification of the NADH-oxidase gene in Trichomonas vaginalis

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