ArticleJournal of bacteriology2011
KefF, the regulatory subunit of the potassium efflux system KefC, shows quinone oxidoreductase activity.
Article in Journal of bacteriology, 2011. 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, 24 citations in OpenAlex.
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- A novel North Sea ammonia-oxidizing archaeon Nitrosarchaeum marinum leverages a high abundance of transport systems to grow over a wide salinity range.FEMS microbiology ecology · 2026Article
- Beyond contact toxicity: Volatile and systemic nematode suppression by 'Journal of nematology · 2026Article
- Structure and mechanism of the KNature communications · 2024Article
- The Potassium Efflux System Kef: Bacterial Protection against Toxic Electrophilic Compounds.Membranes · 2023Review
- Article
- Heme A Synthase Deficiency Affects the Ability ofInternational journal of molecular sciences · 2022Article
- Genetic and molecular characterization of multicomponent resistance ofLife science alliance · 2020Article
- Comparative genomics analysis of Nitriliruptoria reveals the genomic differences and salt adaptation strategies.Extremophiles : life under extreme conditions · 2020Article
- Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System.Biochemistry · 2017Article
- Adaptation, ecology, and evolution of the halophilic stromatolite archaeon Halococcus hamelinensis inferred through genome analyses.Archaea (Vancouver, B.C.) · 2015Article
- Article
- Regulation of ion channels by pyridine nucleotides.Circulation research · 2013Review
- MexT functions as a redox-responsive regulator modulating disulfide stress resistance in Pseudomonas aeruginosa.Journal of bacteriology · 2012Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Escherichia coli and many other Gram-negative pathogenic bacteria protect themselves from the toxic effects of electrophilic compounds by using a potassium efflux system (Kef). Potassium efflux is coupled to the influx of protons, which lowers the internal pH and results in immediate protection. The activity of the Kef system is subject to complex regulation by glutathione and its S conjugates. Full activation of KefC requires a soluble ancillary protein, KefF. This protein has structural similarities to oxidoreductases, including human quinone reductases 1 and 2. Here, we show that KefF has enzymatic activity as an oxidoreductase, in addition to its role as the KefC activator. It accepts NADH and NADPH as electron donors and quinones and ferricyanide (in addition to other compounds) as acceptors. However, typical electrophilic activators of the Kef system, e.g., N-ethyl maleimide, are not substrates. If the enzymatic activity is disrupted by site-directed mutagenesis while retaining structural integrity, KefF is still able to activate the Kef system, showing that the role as an activator is independent of the enzyme activity. Potassium efflux assays show that electrophilic quinones are able to activate the Kef system by forming S conjugates with glutathione. Therefore, it appears that the enzymatic activity of KefF diminishes the redox toxicity of quinones, in parallel with the protection afforded by activation of the Kef system.
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