ArticleJournal of bacteriology2006
WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- Metabolic engineering of Escherichia coli BW25113 for the production of Vitamin KJournal of biological engineering · 2026Article
- A roadmap to chemically reactive species: how diverse oxidants affectMicrobiology and molecular biology reviews : MMBR · 2025Review
- Nature-Inspired Compounds Targeting Escherichia coli WrbA as Biofilm-Modulating Agents: Computational Design, Synthesis, and Biological Evaluation.Archiv der Pharmazie · 2025Article
- Biotechnological potential of silver nanoparticles synthesized by green method to control phytopathogenic bacteria: contributions from a proteomic analysis.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- RpoS and the bacterial general stress response.Microbiology and molecular biology reviews : MMBR · 2024Review
- Unlocking the Antibiofilm Potential of Natural Compounds by Targeting the NADH:quinone Oxidoreductase WrbA.Antioxidants (Basel, Switzerland) · 2023Article
- Mechanistic Insights into the Antibiofilm Mode of Action of Ellagic Acid.Pharmaceutics · 2023Article
- NaturalizedFrontiers in microbiology · 2022Review
- An Assay to Determine NAD(P)H: Quinone Oxidoreductase Activity in Cell Extracts fromBio-protocol · 2021Article
- Effects of the Quinone Oxidoreductase WrbA onAntioxidants (Basel, Switzerland) · 2021Article
- Plasma membrane phylloquinone biosynthesis in nonphotosynthetic parasitic plants.Plant physiology · 2021Article
- Differential Roles of a Family of Flavodoxin-Like Proteins That Promote Resistance to Quinone-Mediated Oxidative Stress in Candida albicans.Infection and immunity · 2021Article
- Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria.Nature communications · 2021Article
- An aspartyl protease-mediated cleavage regulates structure and function of a flavodoxin-like protein and aids oxidative stress survival.PLoS pathogens · 2021Article
- Development of Resistance inAntibiotics (Basel, Switzerland) · 2020Article
- Gene duplication drives genome expansion in a major lineage of Thaumarchaeota.Nature communications · 2020Article
- Adaptive evolution reveals a tradeoff between growth rate and oxidative stress during naphthoquinone-based aerobic respiration.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase.Protein science : a publication of the Protein Society · 2019Article
- Evolutionary Relationships Between Low Potential Ferredoxin and Flavodoxin Electron Carriers.Frontiers in energy research · 2019Article
- Metabolic Engineering of Bacterial Respiration: High vs. Low P/O and the Case ofFrontiers in bioengineering and biotechnology · 2019Review
5 more citing papers are in PubMed but not listed here.
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
WrbA (tryptophan [W] repressor-binding protein) was discovered in Escherichia coli, where it was proposed to play a role in regulation of the tryptophan operon; however, this has been put in question, leaving the function unknown. Here we report a phylogenetic analysis of 30 sequences which indicated that WrbA is the prototype of a distinct family of flavoproteins which exists in a diversity of cell types across all three domains of life and includes documented NAD(P)H:quinone oxidoreductases (NQOs) from the Fungi and Viridiplantae kingdoms. Biochemical characterization of the prototypic WrbA protein from E. coli and WrbA from Archaeoglobus fulgidus, a hyperthermophilic species from the Archaea domain, shows that these enzymes have NQO activity, suggesting that this activity is a defining characteristic of the WrbA family that we designate a new type of NQO (type IV). For E. coli WrbA, the K(m)(NADH) was 14 +/- 0.43 microM and the K(m)(benzoquinone) was 5.8 +/- 0.12 microM. For A. fulgidus WrbA, the K(m)(NADH) was 19 +/- 1.7 microM and the K(m)(benzoquinone) was 37 +/- 3.6 microM. Both enzymes were found to be homodimeric by gel filtration chromatography and homotetrameric by dynamic light scattering and to contain one flavin mononucleotide molecule per monomer. The NQO activity of each enzyme is retained over a broad pH range, and apparent initial velocities indicate that maximal activities are comparable to the optimum growth temperature for the respective organisms. The results are discussed and implicate WrbA in the two-electron reduction of quinones, protecting against oxidative stress.
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