ArticleThe Journal of biological chemistry2010
Direct measurements of the outer membrane stage of ferric enterobactin transport: postuptake binding.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Siderophore-mediated iron acquisition byJournal of bacteriology · 2024Article
- Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu.Frontiers in microbiology · 2024Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- Interaction analyses based on growth parameters of GWAS between Escherichia coli and Staphylococcus aureus.AMB Express · 2021Article
- Conformational rearrangements in the N-domain ofThe Journal of biological chemistry · 2020Article
- Lsr operon is associated with AI-2 transfer and pathogenicity in avian pathogenic Escherichia coli.Veterinary research · 2019Article
- Universal fluorescent sensors of high-affinity iron transport, applied to ESKAPE pathogens.The Journal of biological chemistry · 2019Article
- Stenotrophomonas maltophilia produces an EntC-dependent catecholate siderophore that is distinct from enterobactin.Microbiology (Reading, England) · 2017Article
- Fluorescence High-Throughput Screening for Inhibitors of TonB Action.Journal of bacteriology · 2017Article
- Gating of TonB-dependent transporters by substrate-specific forced remodelling.Nature communications · 2017Article
- TonB-Dependent Heme/Hemoglobin Utilization by Caulobacter crescentus HutA.Journal of bacteriology · 2017Article
- ROSET Model of TonB Action in Gram-Negative Bacterial Iron Acquisition.Journal of bacteriology · 2016Review
- Article
- Identification of a Salmonella ancillary copper detoxification mechanism by a comparative analysis of the genome-wide transcriptional response to copper and zinc excess.Microbiology (Reading, England) · 2014Article
- Concerted loop motion triggers induced fit of FepA to ferric enterobactin.The Journal of general physiology · 2014Article
- The outer membrane TolC-like channel HgdD is part of tripartite resistance-nodulation-cell division (RND) efflux systems conferring multiple-drug resistance in the Cyanobacterium Anabaena sp. PCC7120.The Journal of biological chemistry · 2013Article
- Energy-dependent motion of TonB in the Gram-negative bacterial inner membrane.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The TolC-like protein HgdD of the cyanobacterium Anabaena sp. PCC 7120 is involved in secondary metabolite export and antibiotic resistance.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
When Gram-negative bacteria acquire iron, the metal crosses both the outer membrane (OM) and the inner membrane, but existing radioisotopic uptake assays only measure its passage through the latter bilayer, as the accumulation of the radionuclide in the cytoplasm. We devised a methodology that exclusively observes OM transport and used it to study the uptake of ferric enterobactin (FeEnt) by Escherichia coli FepA. This technique, called postuptake binding, revealed previously unknown aspects of TonB-dependent transport reactions. The experiments showed, for the first time, that despite the discrepancy in cell envelope concentrations of FepA and TonB ( approximately 35:1), all FepA proteins were active and equivalent in FeEnt uptake, with a maximum turnover number of approximately 5/min. FepA-mediated transport of FeEnt progressed through three distinct phases with successively decreasing rates, and from its temperature dependence, the activation energy of the OM stage was 33-35 kcal/mol. The accumulation of FeEnt in the periplasm required the binding protein and inner membrane permease components of its overall transport system; postuptake binding assays on strains devoid of FepB, FepD, or FepG did not show uptake of FeEnt through the OM. However, fluorescence labeling data implied that FepA was active in the DeltafepB strain, suggesting that FeEnt entered the periplasm but then leaked out. Further experiments confirmed this futile cycle; cells without FepB transported FeEnt across the OM, but it immediately escaped through TolC.
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Registered trials
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