ArticleProceedings of the National Academy of Sciences of the United States of America2009
Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 151 citations in OpenAlex.
- Microbiota-Driven Metabolic Alterations Induced by BPA, TDCPP and PFOA in an Ex Vivo Human Fecal Fermentation Model.Chemical research in toxicology · 2026Article
- Iron(III)-Tropolone Complex as a Topical Agent Against Drug-Resistant MRSA Skin Infections.Antibiotics (Basel, Switzerland) · 2026Article
- Biochemical and functional characterization ofFrontiers in microbiology · 2026Article
- The dual implications of iron homeostasis as a bacterial threat: its roles in virulence and antimicrobial resistance.Archives of microbiology · 2025Review
- Commensal gut bacteria employ de-chelatase HmuS to harvest iron from heme.The EMBO journal · 2025Article
- Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers.Biochimica et biophysica acta. Biomembranes · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Comparative Genomic and Functional Analyses for Insights into Pantoea agglomerans Strains Adaptability in Diverse Ecological Niches.Current microbiology · 2024Article
- Bradyrhizobium japonicum HmuP is an RNA-binding protein that positively controls hmuR operon expression by suppression of a negative regulatory RNA element in the 5' untranslated region.Molecular microbiology · 2024Article
- Fluorescence-Based Proteoliposome Methods to Monitor Redox-Active Transition Metal Transmembrane Translocation by Metal Transporters.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The clinical relevance of heme detoxification by the macrophage heme oxygenase system.Frontiers in immunology · 2024Review
- Heme Interactions as Regulators of the Alternative Pathway Complement Responses and Implications for Heme-Associated Pathologies.Current issues in molecular biology · 2023Review
- Enhancement of phycocyanobilin biosynthesis inSynthetic and systems biotechnology · 2023Article
- Microbial Synthesis of HemeMolecules (Basel, Switzerland) · 2023Review
- Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- Transcriptional effects of melatonin on the gut commensal bacterium Klebsiella aerogenes.Genomics · 2022Article
- Harnessing the toxicity of dysregulated iron uptake for killingBiomaterials science · 2022Article
- Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella.EcoSal Plus · 2021Article
- Characterization of Class V DyP-Type Peroxidase SaDyP1 fromInternational journal of molecular sciences · 2021Article
- DyP-Type Peroxidases: Recent Advances and Perspectives.International journal of molecular sciences · 2021Review
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Because heme is a major iron-containing molecule in vertebrates, the ability to use heme-bound iron is a determining factor in successful infection by bacterial pathogens. Until today, all known enzymes performing iron extraction from heme did so through the rupture of the tetrapyrrol skeleton. Here, we identified 2 Escherichia coli paralogs, YfeX and EfeB, without any previously known physiological functions. YfeX and EfeB promote iron extraction from heme preserving the tetrapyrrol ring intact. This novel enzymatic reaction corresponds to the deferrochelation of the heme. YfeX and EfeB are the sole proteins able to provide iron from exogenous heme sources to E. coli. YfeX is located in the cytoplasm. EfeB is periplasmic and enables iron extraction from heme in the periplasm and iron uptake in the absence of any heme permease. YfeX and EfeB are widespread and highly conserved in bacteria. We propose that their physiological function is to retrieve iron from heme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.