ArticleMolecular microbiology2023
NADH dehydrogenases are the predominant phenazine reductases in the electron transport chain of Pseudomonas aeruginosa.
Article in Molecular microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 23 citations in OpenAlex.
- From Planktonic to Sedentary Lifestyle: Molecular Dissection of the Establishment and Maintenance of Mycobacterial Biofilm.ACS omega · 2026Article
- Cellulose-fueled extracellular electron transfer in termite gut microbes.Applied and environmental microbiology · 2026Article
- Genome-wide fitness profiling reveals flagellar rotation as an energetic liability during anaerobic maintenance inbioRxiv : the preprint server for biology · 2026Article
- Deciphering the genetic background of an industrial 2-ketogluconic acid-producing strain Pseudomonas plecoglossicida JUIM01 using whole-genome sequencing.Biotechnology for biofuels and bioproducts · 2026Article
- Redox-dependent lipophilicity of phenazine metabolites is modulated by intramolecular hydrogen bonds and controls their biological distribution.bioRxiv : the preprint server for biology · 2026Article
- Review
- Effects of Organic Substrate Concentrations on Biological Mn Oxidation and Reduction under Aerobic Conditions.Microbes and environments · 2026Article
- Microbial phenazines: biosynthesis, structural diversity, evolution, regulation, and biological significance.Microbiology and molecular biology reviews : MMBR · 2025Review
- Complete uranium bioreduction in 48 hours: Synergistic electron transfer in a synthetic microbial consortium.Environmental science and ecotechnology · 2025Article
- Loss of LasR function leads to decreased repression ofJournal of bacteriology · 2025Article
- Decoding in-cell respiratory enzyme dynamics by label-free in situ electrochemistry.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mutations in the Staphylococcus aureus Global Regulator CodY confer tolerance to an interspecies redox-active antimicrobial.PLoS genetics · 2025Article
- The phospho-ferrozine assay: a tool to study bacterial redox-active metabolites produced at the plant root.Applied and environmental microbiology · 2025Article
- Mechanistic study of a low-power bacterial maintenance state using high-throughput electrochemistry.Cell · 2024Article
- Bioenergetic suppression by redox-active metabolites promotes antibiotic tolerance inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mutations in thebioRxiv : the preprint server for biology · 2024Article
- Genetically dissecting the electron transport chain of a soil bacterium reveals a generalizable mechanism for biological phenazine-1-carboxylic acid oxidation.PLoS genetics · 2024Article
- Article
- Genetically dissecting the electron transport chain of a soil bacterium reveals a generalizable mechanism for biological phenazine-1-carboxylic acid oxidation.bioRxiv : the preprint server for biology · 2023Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Phenazines are redox-active secondary metabolites produced by diverse bacteria including the opportunistic pathogen Pseudomonas aeruginosa. Extracellular electron transfer via phenazines enhances anaerobic survival by serving as an electron sink for glucose catabolism. However, the specific phenazine reductase(s) used to support this catabolism are unknown. Because electron transport chain components have been previously implicated in phenazine reduction, we sought to determine which of them possess phenazine reductase activity. We show that phenazine-1-carboxamide (PCN) and pyocyanin (PYO) are reduced at the highest rate by cells and are localized to the cell envelope while reduced. Using a coupled genetic and biochemical approach, we show that phenazine reductase activity in membrane fractions is attributable to the three NADH dehydrogenases present in P. aeruginosa and that their order of phenazine reductase activity is Nqr > Nuo > Ndh. In mutants possessing only one functional NADH dehydrogenase, whole cell reduction rates of PCN, but not PYO, recapitulate the pattern of biochemical results, implying that PYO reduction is predominantly occurring in the cytosol. Lastly, we show that ubiquinone rapidly and non-enzymatically oxidizes reduced phenazines, demonstrating that phenazines have the capability to serve in a redox loop between the NADH and ubiquinone pools, a finding that carries bioenergetic implications.
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