ArticlePloS one2021
The three NADH dehydrogenases of Pseudomonas aeruginosa: Their roles in energy metabolism and links to virulence.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
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- NQR as a target for new antibiotics.Frontiers in microbiology · 2025Review
- Evaluation of expanded 2-aminobenzothiazole library as inhibitors of a model histidine kinase and virulence suppressors in Pseudomonas aeruginosa.Bioorganic chemistry · 2024Article
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- Metatranscriptomic analysis shows functional alterations in subgingival biofilm in young smokers with periodontitis: a pilot study.Journal of applied oral science : revista FOB · 2024Observational
- Bacterial respiratory inhibition triggers dispersal ofApplied and environmental microbiology · 2023Article
- NADH dehydrogenases are the predominant phenazine reductases in the electron transport chain of Pseudomonas aeruginosa.Molecular microbiology · 2023Article
- Thermal acclimation of methanotrophs from the genus Methylobacter.The ISME journal · 2023Article
- Comparative genomics ofFrontiers in microbiology · 2023Article
- Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022Review
- Genetic and Biochemical Characterization of the NaJournal of bacteriology · 2021Article
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa is a ubiquitous opportunistic pathogen which relies on a highly adaptable metabolism to achieve broad pathogenesis. In one example of this flexibility, to catalyze the NADH:quinone oxidoreductase step of the respiratory chain, P. aeruginosa has three different enzymes: NUO, NQR and NDH2, all of which carry out the same redox function but have different energy conservation and ion transport properties. In order to better understand the roles of these enzymes, we constructed two series of mutants: (i) three single deletion mutants, each of which lacks one NADH dehydrogenase and (ii) three double deletion mutants, each of which retains only one of the three enzymes. All of the mutants grew approximately as well as wild type, when tested in rich and minimal medium and in a range of pH and [Na+] conditions, except that the strain with only NUO (ΔnqrFΔndh) has an extended lag phase. During exponential phase, the NADH dehydrogenases contribute to total wild-type activity in the following order: NQR > NDH2 > NUO. Some mutants, including the strain without NQR (ΔnqrF) had increased biofilm formation, pyocyanin production, and killed more efficiently in both macrophage and mouse infection models. Consistent with this, ΔnqrF showed increased transcription of genes involved in pyocyanin production.
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