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Enterobactin: an archetype for microbial iron transport.
Open accessAbstract
Bacteria have aggressive acquisition processes for iron, an essential nutrient. Siderophores are small iron chelators that facilitate cellular iron transport. The siderophore enterobactin is a triscatechol derivative of a cyclic triserine lactone. Studies of the chemistry, regulation, synthesis, recognition, and transport of enterobactin make it perhaps the best understood of the siderophore-mediated iron uptake systems, displaying a lot of function packed into this small molecule. However, recent surprises include the isolation of corynebactin, a closely related trithreonine triscatechol derivative lactone first found in Gram-positive bacteria, and the crystal structure of a ferric enterobactin complex of a protein identified as an antibacterial component of the human innate immune system.
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“Given the low Fe bioavailability in an aqueous environment (free Fe3+ concentration below 10−9 M at pH 7) and the further strict active withholding of Fe within mammalian hosts (free serum Fe concentration of approximately 10−24 M) [9]”
From Host Iron Withholding Demands Siderophore Utilization for Candida glabrata to Survive Macrophage Killing (2011) · cites this paper as [9]
Citations
Cites
Siderophores: Structure and Function of Microbial Iron Transport Compounds
Neilands, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26723 · Cited by 1,652
Iron Metabolism in Pathogenic Bacteria
Ratledge, C., & Dover, L. G. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.881 · Cited by 1,539
Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Self-citationIsolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
Kjeldsen, L., Johnsen, A., Sengeløv, H., & Borregaard, N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82217-7 · Cited by 1,286
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755
Iron transport in microbes, plants and animals
Danchin, A. (1988) · Biochimie · doi:10.1016/0300-9084(88)90122-8 · Cited by 607
Stoichiometric and site characteristics of the binding of iron to human transferrin
Aisen, P., Leibman, A., & Zweier, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62337-9 · Cited by 601
Bagg, A., & Neilands, J. B. (1987) · Biochemistry · doi:10.1021/bi00391a039 · Cited by 593
Crystal structure of the outer membrane active transporter FepA from Escherichia coli.
Buchanan (1999) · Nature Structural Biology · doi:10.1038/4931 · Cited by 591
Research works printed but not linked: 5
- J J Bullen, L C Leigh, H J Rogers Immunology 15, 581–588 (1968).
- 10.1016/0378-1097(90)90522-R · DOI
- J J Bullen, H J Rogers, J E Lewin Immunology 20, 391–406 (1971).
- A Trousseau Lect Clin Med 5, 95–117 (1872).
- V Braun, K Hantke CRC Handbook of Microbial Iron Chelators, ed G Winkelmann (CRC, Boca Raton, FL), pp. 107–138 (1991).
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Gerc, A. J., Stanley‐Wall, N. R., & Coulthurst, S. J. (2014) · Microbiology · doi:10.1099/mic.0.078576-0 · Cited by 27
Tiwari, V., Rajeswari, M. R., & Tiwari, M. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.12.173 · Cited by 26
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Hong, S., & Lee, E. Y. (2014) · International Biodeterioration & Biodegradation · doi:10.1016/j.ibiod.2014.05.026 · Cited by 21
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Khalil, S., & Pawelek, P. D. (2010) · Biochemistry · doi:10.1021/bi101558v · Cited by 20
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Guo, C., Steinberg, L. K., Henderson, J. P., & Gross, M. L. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02194 · Cited by 20
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Sánchez, S., Guzmán‐Trampe, S., Ávalos, M., Ruiz‐Villafán, B., Rodrı́guez-Sanoja, R., & Jiménez‐Estrada, M. (2012) · Wiley eBooks · doi:10.1002/9781118391815.ch3 · Cited by 20
Wu, Y., Yang, Y., Dang, H., Xiao, H., Huang, W., Jia, Z., Zhao, X., Chen, K., Ji, N., Guo, J., et al. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.10.002 · Cited by 19
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Gómez‐Casado, C., Roth‐Walter, F., Jensen‐Jarolim, E., Díaz‐Perales, A., & Pacios, L. F. (2013) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2013.08.013 · Cited by 19
Constable, E. C., Zhang, G., Housecroft, C. E., Neuburger, M. A., & Schaffner, S. (2009) · Dalton Transactions · doi:10.1039/b916996m · Cited by 19
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Metadata
- Authors
- Raymond, K. N., Dertz, E. A., & Kim, S. S.
- Affiliations
- University of California, Berkeley (US)
- ORCID
- Raymond, Kenneth N.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-03-24
- Volume
- 100
- Issue
- 7
- Pages
- 3584-3588
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC152965
- OpenAlex
- W1972422447
- Cited by
- 933
- References
- 83
- Citations by year
- 2026: 42 · 2025: 57 · 2024: 55 · 2023: 47 · 2022: 67 · 2021: 46 · 2020: 49 · 2019: 59 · 2018: 50 · 2017: 47 · 2016: 38 · 2015: 38 · 2014: 47 · 2013: 27 · 2012: 45
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R01AI011744, AI-11744)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- enterobactin, siderophores, bacterial iron acquisition, iron transport, siderophore biosynthesis, innate immunity, Gram-positive bacteria
- MeSH terms
- Bacteria, Binding Sites, Carrier Proteins, Enterobactin, Iron, Models, Molecular, Protein Conformation, Protein Structure, Secondary
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