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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Free Fe3+ concentration is below 10−9 M at pH 7 and free serum Fe concentration is approximately 10−24 M.
“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]
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755 · see citing works
Iron transport in microbes, plants and animals
Danchin, A. (1988) · Biochimie · doi:10.1016/0300-9084(88)90122-8 · Cited by 607 · see citing works
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 · see citing works
Bagg, A., & Neilands, J. B. (1987) · Biochemistry · doi:10.1021/bi00391a039 · Cited by 593 · see citing works
Crystal structure of the outer membrane active transporter FepA from Escherichia coli.
Buchanan (1999) · Nature Structural Biology · doi:10.1038/4931 · Cited by 591 · see citing works
Iron carriers and iron proteins
Loehr, T. M. (1989) · Medical Entomology and Zoology · Cited by 436 · see citing works
Enterobactin, an iron transport compound from Salmonella typhimurium
Pollack, J. R., & Neilands, J. B. (1970) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(70)90819-3 · Cited by 433 · see citing works
Nielsen, B. S., Borregaard, N., Bundgaard, J. R., Timshel, S., Sehested, M., & Kjeldsen, L. (1996) · Gut · doi:10.1136/gut.38.3.414 · Cited by 422 · see citing works
Bacterial solutions to the iron-supply problem
Braun, V., & Killmann, H. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01359-6 · Cited by 407 · see citing works
Iron transport in microbes, plants, and animals
Winkelmann, G., der Helm, D. V., & Neilands, J. B. (1987) · Cited by 380 · see citing works
Devireddy, L. R., Teodoro, J. G., Richard, F. A., & Green, M. R. (2001) · Science · doi:10.1126/science.1061075 · Cited by 379 · see citing works
The structure of enterochelin and related 2,3-dihydroxy-N-benzoyne conjugates from Eschericha Coli
O'Brien, I. G., & Gibson, F. (1970) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(70)90038-3 · Cited by 366 · see citing works
May, J. J., Wendrich, T. M., & Marahiel, M. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009140200 · Cited by 359 · see citing works
Role of iron in the pathogenesis of Vibrio vulnificus infections
Wright, A. C., Simpson, L. M., & Oliver, J. D. (1981) · Infection and Immunity · doi:10.1128/iai.34.2.503-507.1981 · Cited by 343 · see citing works
Bacterial iron transport: mechanisms, genetics, and regulation.
Braun, V., Hantke, K., & Köster, W. L. (1998) · PubMed · Cited by 294 · see citing works
Coordination chemistry and microbial iron transport
Raymond, K. N., & Carrano, C. J. (1979) · Accounts of Chemical Research · doi:10.1021/ar50137a004 · Cited by 293 · see citing works
Self-citationEffects of iron and desferrioxamine on infections with Yersinia enterocolitica
Robins-Browne, R. M., & Prpic, J. K. (1985) · Infection and Immunity · doi:10.1128/iai.47.3.774-779.1985 · Cited by 266 · see citing works
Iron uptake mechanisms and their regulation in pathogenic bacteria
Braun, V. (2001) · International Journal of Medical Microbiology · doi:10.1078/1438-4221-00103 · Cited by 249 · see citing works
Gehring, A. M., Bradley, K. A., & Walsh, C. T. (1997) · Biochemistry · doi:10.1021/bi970453p · Cited by 226 · see citing works
Transferrin binding of Al3+ and Fe3+.
Martin, R. B., Savory, J., Brown, S., Bertholf, R. L., & Wills, M. R. (1987) · Clinical Chemistry · doi:10.1093/clinchem/33.3.405 · Cited by 217 · see citing works
Molecular studies on enzymes in chorismate metabolism and the enterobactin biosynthetic pathway
Walsh, C. T., Liu, J. O., Rusnak, F. M., & Sakaitani, M. (1990) · Chemical Reviews · doi:10.1021/cr00105a003 · Cited by 213 · see citing works
Cloning of the repressor protein gene of iron-regulated systems in Escherichia coli K12
Hantke, K. (1984) · Molecular and General Genetics MGG · doi:10.1007/bf00330982 · Cited by 204 · see citing works
Ligand Preference Inferred from the Structure of Neutrophil Gelatinase Associated Lipocalin
Goetz, D. H., Willie, S. T., Armen, R. S., Bratt, T., Borregaard, N., & Strong, R. K. (2000) · Biochemistry · doi:10.1021/bi992215v · Cited by 184 · see citing works
Ernst, J., Bennett, R. L., & Rothfield, L. I. (1978) · Journal of Bacteriology · doi:10.1128/jb.135.3.928-934.1978 · Cited by 174 · see citing works
Brickman, T. J., & McIntosh, M. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49846-3 · Cited by 167 · see citing works
Shaw-Reid, C. A., Kelleher, N. L., Losey, H. C., Gehring, A. M., Berg, C., & Walsh, C. T. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80050-7 · Cited by 163 · see citing works
Increased Incidence of Gram-Negative Neonatal Sepsis With Intramuscular Iron Administration
Barry, D. M., & Reeve, A. W. (1977) · PEDIATRICS · doi:10.1542/peds.60.6.908 · Cited by 157 · see citing works
Molecular and Cellular Iron Transport
(2002) · CRC Press eBooks · doi:10.1201/9780824744175.fmatt1 · Cited by 150 · see citing works
Rusnak, F. M., Sakaitani, M., Drueckhammer, D. G., Reichert, J. M., & Walsh, C. T. (1991) · Biochemistry · doi:10.1021/bi00225a027 · Cited by 147 · see citing works
Mechanisms of iron acquisition and bacterial virulence
MartÃnez, J. L., Delgado‐Iribarren, A., & Baquero, F. (1990) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1990.tb04085.x · Cited by 146 · see citing works
Increased incidence of gram-negative neonatal sepsis with intramuscula iron administration.
Barry, D. M., & Reeve, A. W. (1977) · PubMed · Cited by 143 · see citing works
Iron, DtxR, and the regulation of diphtheria toxin expression
Tao, X., Schiering, N., Zeng, H., Ringe, D., & Murphy, J. R. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01280.x · Cited by 143 · see citing works
Ozenberger, B. A., Brickman, T. J., & McIntosh, M. A. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.775-783.1989 · Cited by 118 · see citing works
Stack, T. D. P., Hou, Z., & Raymond, K. N. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00067a094 · Cited by 111 · see citing works
Self-citationEffect of serum albumin on siderophore-mediated utilization of transferrin iron
Konopka, K., & Neilands, J. B. (1984) · Biochemistry · doi:10.1021/bi00305a003 · Cited by 108 · see citing works
Karpishin, T. B., Dewey, T. M., & Raymond, K. N. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00058a032 · Cited by 108 · see citing works
Self-citationThe effect of iron compounds on the virulence of Escherichia coli for guinea-pigs.
Bullen, J. J., Leigh, L. C., & Rogers, H. J. (1968) · PubMed · Cited by 108 · see citing works
Iron and its sensitive balance in the cell
Freitas, J. M. D., & Meneghini, R. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00066-5 · Cited by 101 · see citing works
Fiedler, H., Krastel, P., Müller, J., Gebhardt, K., & Zeeck, A. (2001) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2001.tb10556.x · Cited by 91 · see citing works
Effect of loop deletions on the binding and transport of ferric enterobactin by FepA
Newton, S. M. C., Igo, J. D., Scott, D. C., & Klebba, P. E. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01424.x · Cited by 91 · see citing works
Iron and bacterial virulence–a brief overview.
Griffiths, E. (1991) · Biology of Metals · doi:10.1007/bf01135551 · Cited by 86 · see citing works
Recognition and transport of ferric enterobactin in Escherichia coli
Ecker, D. J., Matzanke, B. F., & Raymond, K. N. (1986) · Journal of Bacteriology · doi:10.1128/jb.167.2.666-673.1986 · Cited by 86 · see citing works
Self-citationSynthesis of iron chelators. Enterobactin, enantioenterobactin, and a chiral analog
Rastetter, W. H., Erickson, T. J., & Venuti, M. C. (1981) · The Journal of Organic Chemistry · doi:10.1021/jo00331a001 · Cited by 86 · see citing works
Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease
Chenault, S. S., & Earhart, C. F. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb00787.x · Cited by 83 · see citing works
Binding of Ferric Enterobactin by theEscherichia coliPeriplasmic Protein FepB
Sprencel, C., Cao, Z., Qi, Z., Scott, D. C., Montague, M. A., Ivanoff, N., Xu, J., Raymond, K., Newton, S. M. C., & Klebba, P. E. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.19.5359-5364.2000 · Cited by 82 · see citing works
Self-citationIron and Infection: Molecular, physiological and clinical aspects
WILLIAMS, P. H. (1988) · Biochemical Society Transactions · doi:10.1042/bst0160078a · Cited by 78 · see citing works
Stereospecificity of the ferric enterobactin receptor of Escherichia coli K-12.
Neilands, J. B., Erickson, T. J., & Rastetter, W. H. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69531-1 · Cited by 77 · see citing works
Selectivity of Ferric Enterobactin Binding and Cooperativity of Transport in Gram-Negative Bacteria
Thulasiraman, P., Newton, S. M. C., Xu, J., Raymond, K. N., Mai, C., Hall, A., Montague, M. A., & Klebba, P. E. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.24.6689-6696.1998 · Cited by 74 · see citing works
Self-citationWyckoff, E. E., Valle, A.-M., Smith, S. L., & Payne, S. M. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.24.7588-7596.1999 · Cited by 74 · see citing works
Bidlack, W. R. (1999) · Journal of the American College of Nutrition · doi:10.1080/07315724.1999.10718833 · Cited by 72 · see citing works
The critical role of iron in some clinical infections
Bullen, J. J., Ward, C., & Rogers, H. J. (1991) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/bf01975810 · Cited by 72 · see citing works
The First Structural Characterization of a Metal–Enterobactin Complex: [V(enterobactin)]2−
Karpishin, T. B., & Raymond, K. N. (1992) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199204661 · Cited by 71 · see citing works
Self-citationStack, T. D. P., Karpishin, T. B., & Raymond, K. N. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00030a075 · Cited by 71 · see citing works
Self-citationMeyer, M., Telford, J. R., Cohen, S. M., White, D. J., Xu, J., & Raymond, K. N. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970718n · Cited by 70 · see citing works
Self-citationIron(III) coordination chemistry of linear dihydroxyserine compounds derived from enterobactin
Scarrow, R. C., Ecker, D. J., Ng, C. Y., Liu, S., & Raymond, K. N. (1991) · Inorganic Chemistry · doi:10.1021/ic00005a007 · Cited by 68 · see citing works
Self-citationUsher, K. C., Özkan, E., Gardner, K. H., & Deisenhofer, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181353398 · Cited by 67 · see citing works
Hou, Z., Stack, T. D. P., Sunderland, C. J., & Raymond, K. N. (1997) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(97)05664-8 · Cited by 64 · see citing works
Self-citationTotal synthesis of enterobactin, a macrocyclic iron transporting agent of bacteria
Corey, E. J., & Bhattacharyya, S. (1977) · Tetrahedron Letters · doi:10.1016/s0040-4039(01)83390-6 · Cited by 62 · see citing works
Nahlik, M. S., Fleming, T. P., & McIntosh, M. A. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.9.4163-4170.1987 · Cited by 61 · see citing works
Hemoglobin and <i>Escherichia coli</i> , a Lethal Intraperitoneal Combination
Bornside, G. H., Bouis, P. J., & Cohn, I. (1968) · Journal of Bacteriology · doi:10.1128/jb.95.5.1567-1571.1968 · Cited by 57 · see citing works
Iron and virulence in <i>Shigella</i>
Payne, S. M. (1989) · Molecular Microbiology · doi:10.1111/j.1365-2958.1989.tb00281.x · Cited by 57 · see citing works
The bacteriostatic effect of serum on Pasteurella septica and its abolition by iron compounds.
Bullen, J. J., Rogers, H. J., & Lewin, J. E. (1971) · PubMed · Cited by 53 · see citing works
Effect of iron compounds on antibacterial function of human polymorphs and plasma
Ward, C., Hammond, J. S., & Bullen, J. J. (1986) · Infection and Immunity · doi:10.1128/iai.51.3.723-730.1986 · Cited by 52 · see citing works
Seebàch, D., Müller, H., Bürger, H. M., & Plattner, D. A. (1992) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199204341 · Cited by 51 · see citing works
Corynebactin and Enterobactin: Related Siderophores of Opposite Chirality
Bluhm, M. E., Kim, S. S., Dertz, E. A., & Raymond, K. N. (2002) · Journal of the American Chemical Society · doi:10.1021/ja016651s · Cited by 45 · see citing works
Self-citationAromatic components of two ferric enterobactin binding sites in <i>Escherichia coli</i> FepA
Cao, Z., Qi, Z., Sprencel, C., Newton, S. M. C., & Klebba, P. E. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02093.x · Cited by 45 · see citing works
Characterization of EntF as a serine‐activating enzyme
Reichert, J. M., Sakaitani, M., & Walsh, C. T. (1992) · Protein Science · doi:10.1002/pro.5560010410 · Cited by 44 · see citing works
Greenwood, K. T., & Luke, R. K. J. (1978) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(78)90216-4 · Cited by 44 · see citing works
Total synthesis of enterobactin via an organotin template
Shanzer, A., & Libman, J. (1983) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39830000846 · Cited by 44 · see citing works
The spectroelectrochemical determination of the reduction potential of differic serum transferrin
Kretchmar, S. A., Reyes, Z. E., & Raymond, K. N. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90301-9 · Cited by 43 · see citing works
Self-citationCorynebactin, a Cyclic Catecholate Siderophore from
Budzikiewicz, H., Bössenkamp, A., Taraz, K., Pandey, A., & Meyer, J. (1997) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1997-7-820 · Cited by 42 · see citing works
Tse, B., & Kishi, Y. (1994) · The Journal of Organic Chemistry · doi:10.1021/jo00104a043 · Cited by 35 · see citing works
A much improved synthesis of the siderophore enterobactin
Ramirez, R. J. A., Karamanukyan, L., Ortiz, S., & Gutierrez, C. G. (1997) · Tetrahedron Letters · doi:10.1016/s0040-4039(96)02452-5 · Cited by 35 · see citing works
Bluhm, M. E., Hay, B. P., Kim, S. S., Dertz, E. A., & Raymond, K. N. (2002) · Inorganic Chemistry · doi:10.1021/ic025531y · Cited by 29 · see citing works
Self-citationChart, H., & Griffiths, E. (1985) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1985.tb01596.x · Cited by 23 · see citing works
Flagged first, then by citations
3 of the 83 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Siderophore-Based Iron Acquisition and Pathogen Control
Miethke, M., & Marahiel, M. A. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-07 · Cited by 1,774 · see citing works
Chemistry and biology of siderophores
Hider, R. C., & Kong, X. (2010) · Natural Product Reports · doi:10.1039/b906679a · Cited by 1,722 · see citing works
Bioinspired catecholic chemistry for surface modification
Ye, Q., Zhou, F., & Liu, W. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15026j · Cited by 1,177 · see citing works
Bacterial Iron Sources: From Siderophores to Hemophores
Wandersman, C., & Delepelaire, P. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123811 · Cited by 1,056 · see citing works
Nonribosomal Peptide Synthesis—Principles and Prospects
Süßmuth, R. D., & Mainz, A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201609079 · Cited by 950 · see citing works
(2011) · Cited by 918 · see citing works
Catechol‐Based Biomimetic Functional Materials
Sedó, J., Saiz‐Poseu, J., Busquè, F., & Ruiz‐Molina, D. (2012) · Advanced Materials · doi:10.1002/adma.201202343 · Cited by 755 · see citing works
Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
Maier, G. P., Rapp, M. V., Waite, J. H., Israelachvili, J. N., & Butler, A. (2015) · Science · doi:10.1126/science.aab0556 · Cited by 722 · see citing works
Metals to combat antimicrobial resistance
Frei, A., Verderosa, A. D., Elliott, A. G., Zuegg, J., & Blaskovich, M. A. T. (2023) · Nature Reviews Chemistry · doi:10.1038/s41570-023-00463-4 · Cited by 656 · see citing works
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598 · see citing works
New roles for bacterial siderophores in metal transport and tolerance
Schalk, I. J., Hannauer, M., & Braud, A. (2011) · Environmental Microbiology · doi:10.1111/j.1462-2920.2011.02556.x · Cited by 583 · see citing works
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Probiotic Bacteria Reduce Salmonella Typhimurium Intestinal Colonization by Competing for Iron
Deriu, E., Liu, J. Z., Pezeshki, M., Edwards, R. A., Ochoa, R. J., Contreras, H., Libby, S. J., Fang, F. C., & Raffatellu, M. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.007 · Cited by 550 · see citing works
The outer mucus layer hosts a distinct intestinal microbial niche
Li, H., Limenitakis, J. P., Fuhrer, T., Geuking, M. B., Lawson, M. A., Wyss, M., Brugiroux, S., Keller, I., Macpherson, J. A., Rupp, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9292 · Cited by 511 · see citing works
Lee, C.-R., Lee, J. H., Park, K. S., Jeon, J. H., Kim, Y. B., Cha, C., Jeong, B. C., & Lee, S. H. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00483 · Cited by 496 · see citing works
Microbial Iron Acquisition: Marine and Terrestrial Siderophores
Sandy, M., & Butler, A. (2009) · Chemical Reviews · doi:10.1021/cr9002787 · Cited by 490 · see citing works
Yu, X. M., Ai, C., Li, X., & Zhou, G. (2010) · European Journal of Soil Biology · doi:10.1016/j.ejsobi.2010.11.001 · Cited by 468 · see citing works
Microbial siderophores: a mini review
Saha, R., Saha, N., Donofrio, R. S., & Bestervelt, L. L. (2012) · Journal of Basic Microbiology · doi:10.1002/jobm.201100552 · Cited by 438 · see citing works
Characterization and Biological Function of the ISOCHORISMATE SYNTHASE2 Gene of Arabidopsis
Garcion, C., Lohmann, A., Lamodière, E., Catinot, J., Buchala, A. J., Dörmann, P., & Métraux, J. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.119420 · Cited by 421 · see citing works
Neutrophil gelatinase-associated lipocalin as the real-time indicator of active kidney damage
Mori, K., & Nakao, K. (2007) · Kidney International · doi:10.1038/sj.ki.5002165 · Cited by 415 · see citing works
Synthesis, nature and utility of universal iron chelator – Siderophore: A review
Khan, A., Singh, P., & Srivastava, A. (2017) · Microbiological Research · doi:10.1016/j.micres.2017.10.012 · Cited by 412 · see citing works
Beyond iron: non-classical biological functions of bacterial siderophores
Johnstone, T. C., & Nolan, E. M. (2015) · Dalton Transactions · doi:10.1039/c4dt03559c · Cited by 410 · see citing works
Bell, K. S., Sebaihia, M., Pritchard, L., Holden, M. T. G., Hyman, L. J., Holeva, M. C., Thomson, N. R., Bentley, S. D., Churcher, L. J. C., Mungall, K., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402424101 · Cited by 408 · see citing works
Nonproteinogenic Amino Acid Building Blocks for Nonribosomal Peptide and Hybrid Polyketide Scaffolds
Walsh, C. T., O’Brien, R. V., & Khosla, C. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208344 · Cited by 408 · see citing works
Karampatakis, T., Tsergouli, K., & Behzadi, P. (2023) · Antibiotics · doi:10.3390/antibiotics12020234 · Cited by 369 · see citing works
Guo, Y., Nguyen, K.-A. T., & Potempa, J. (2010) · Periodontology 2000 · doi:10.1111/j.1600-0757.2010.00377.x · Cited by 367 · see citing works
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
New substrates for TonB-dependent transport: do we only see the ‘tip of the iceberg’?
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Iron in infection and immunity
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Chu, B. C. H., Garcia-Herrero, A., Johanson, T. H., Krewulak, K. D., Lau, C. K. Y., Peacock, R. S., Slavinskaya, Z., & Vogel, H. J. (2010) · BioMetals · doi:10.1007/s10534-010-9361-x · Cited by 339 · see citing works
Timofeeva, A. M., Galyamova, M. R., & Sedykh, S. E. (2023) · Plants · doi:10.3390/plants12244074 · Cited by 336 · see citing works
Cotruvo, J. A. (2019) · ACS Central Science · doi:10.1021/acscentsci.9b00642 · Cited by 325 · see citing works
Bacterial Siderophores: Classification, Biosynthesis, Perspectives of Use in Agriculture
Timofeeva, A. M., Galyamova, M. R., & Sedykh, S. E. (2022) · Plants · doi:10.3390/plants11223065 · Cited by 324 · see citing works
How pathogenic bacteria evade mammalian sabotage in the battle for iron
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2006) · Nature Chemical Biology · doi:10.1038/nchembio771 · Cited by 321 · see citing works
The pathogen-associated <i>iroA</i> gene cluster mediates bacterial evasion of lipocalin 2
Fischbach, M. A., Lin, H., Zhou, L., Yu, Y., Abergel, R. J., Liu, D. R., Raymond, K. N., Wanner, B. L., Strong, R. K., Walsh, C. T., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604636103 · Cited by 319 · see citing works
Self-citationGut Microbiota and Iron: The Crucial Actors in Health and Disease
Yilmaz, B., & Li, H. (2018) · Pharmaceuticals · doi:10.3390/ph11040098 · Cited by 317 · see citing works
Structure, activity, synthesis and biosynthesis of aryl-C-glycosides
Bililign, T., Griffith, B. R., & Thorson, J. S. (2005) · Natural Product Reports · doi:10.1039/b407364a · Cited by 306 · see citing works
Sivasakthi, S., Usharani, G., & Saranraj, P. (2014) · African Journal of Agricultural Research · doi:10.5897/ajar2013.7914 · Cited by 303 · see citing works
Devireddy, L. R., Hart, D. O., Goetz, D. H., & Green, M. R. (2010) · Cell · doi:10.1016/j.cell.2010.04.040 · Cited by 295 · see citing works
Coordination Chemistry of Microbial Iron Transport
Raymond, K. N., Allred, B. E., & Sia, A. K. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00301 · Cited by 292 · see citing works
Self-citationNutritional iron turned inside out: intestinal stress from a gut microbial perspective
Kortman, G. A. M., Raffatellu, M., Swinkels, D. W., & Tjalsma, H. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12086 · Cited by 291 · see citing works
Bacterial survival strategies and responses under heavy metal stress: a comprehensive overview
Pal, A., Bhattacharjee, S., Saha, J., Sarkar, M. P., & Mandal, P. (2021) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2021.1970512 · Cited by 284 · see citing works
Siderophores as drug delivery agents: application of the “Trojan Horse” strategy
Möllmann, U., Heinisch, L., Bauernfeind, A., Köhler, T., & Ankel‐Fuchs, D. (2009) · BioMetals · doi:10.1007/s10534-009-9219-2 · Cited by 275 · see citing works
Recent developments in understanding the iron acquisition strategies of gram positive pathogens
Sheldon, J. R., & Heinrichs, D. E. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv009 · Cited by 272 · see citing works
Resistance and survival strategies of Salmonella enterica to environmental stresses
Spector, M. P., & Kenyon, W. J. (2011) · Food Research International · doi:10.1016/j.foodres.2011.06.056 · Cited by 268 · see citing works
Yersiniabactin Is a Virulence Factor for Klebsiella pneumoniae during Pulmonary Infection
Lawlor, M. S., O'Connor, C., & Miller, V. L. (2007) · Infection and Immunity · doi:10.1128/iai.00372-06 · Cited by 255 · see citing works
Pseudomonas syringae pv. actinidiae : a re‐emerging, multi‐faceted, pandemic pathogen
Scortichini, M., Marcelletti, S., Ferrante, P., Petriccione, M., & Firrao, G. (2012) · Molecular Plant Pathology · doi:10.1111/j.1364-3703.2012.00788.x · Cited by 254 · see citing works
Bacterial siderophores: diversity, uptake pathways and applications
Schalk, I. J. (2024) · Nature Reviews Microbiology · doi:10.1038/s41579-024-01090-6 · Cited by 248 · see citing works
Braud, A., Hoegy, F., Jezequel, K., Lebeau, T., & Schalk, I. J. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2008.01838.x · Cited by 246 · see citing works
Holmes, M. A., Paulsene, W., Jide, X., Ratledge, C., & Strong, R. K. (2005) · Structure · doi:10.1016/j.str.2004.10.009 · Cited by 246 · see citing works
Synthetic and natural iron chelators: Therapeutic potential and clinical use
Hatcher, H. C., Singh, R. N., Torti, F. M., & Torti, S. V. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.121 · Cited by 242 · see citing works
Polyphenol‐Induced Adhesive Liquid Metal Inks for Substrate‐Independent Direct Pen Writing
Rahim, M. A., Centurion, F., Han, J., Abbasi, R., Mayyas, M., Sun, J., Christoe, M. J., Esrafilzadeh, D., Allioux, F., Ghasemian, M. B., et al. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202007336 · Cited by 242 · see citing works
Chillappagari, S., Seubert, A., Trip, H., Kuipers, O. P., Marahiel, M. A., & Miethke, M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00058-10 · Cited by 239 · see citing works
Neutrophil gelatinase-associated lipocalin-mediated iron traffic in kidney epithelia
Schmidt-Ott, K. M., Mori, K., Kalandadze, A., Li, J.-Y., Paragas, N., Nicholas, T., Devarajan, P., & Barasch, J. (2006) · Current Opinion in Nephrology & Hypertension · doi:10.1097/01.mnh.0000232886.81142.58 · Cited by 237 · see citing works
Henderson, J. P., Crowley, J. R., Pinkner, J. S., Walker, J. N., Tsukayama, P., Stamm, W. E., Hooton, T. M., & Hultgren, S. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000305 · Cited by 231 · see citing works
Iron-binding properties of plant phenolics and cranberry's bio-effects
Guo, M., Perez, C., Wei, Y., Rapoza, E., Su, G. M., Bou‐Abdallah, F., & Chasteen, N. D. (2007) · Dalton Transactions · doi:10.1039/b705136k · Cited by 227 · see citing works
The shikimate pathway: gateway to metabolic diversity
Shende, V. V., Bauman, K. D., & Moore, B. S. (2024) · Natural Product Reports · doi:10.1039/d3np00037k · Cited by 216 · see citing works
Brandel, J., Humbert, N., Elhabiri, M., Schalk, I. J., Mislin, G. L. A., & Albrecht‐Gary, A. (2012) · Dalton Transactions · doi:10.1039/c1dt11804h · Cited by 214 · see citing works
Waging War against UropathogenicEscherichia coli: Winning Back the Urinary Tract
Sivick, K. E., & Mobley, H. L. T. (2009) · Infection and Immunity · doi:10.1128/iai.01000-09 · Cited by 214 · see citing works
The Pseudomonas aeruginosa Pyochelin-Iron Uptake Pathway and Its Metal Specificity
Braud, A., Hannauer, M., Mislin, G. L. A., & Schalk, I. J. (2009) · Journal of Bacteriology · doi:10.1128/jb.00010-09 · Cited by 211 · see citing works
Abbas, R., Chakkour, M., Dine, H. Z. E., Obaseki, E., Obeid, S. T., Jezzini, A., Ghssein, G., & Ezzeddine, Z. (2024) · Biology · doi:10.3390/biology13020078 · Cited by 212 · see citing works
Siderophores: Importance in bacterial pathogenesis and applications in medicine and industry
Khasheii, B., Mahmoodi, P., & Mohammadzadeh, A. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126790 · Cited by 210 · see citing works
Role of the Fur Regulon in Iron Transport in Bacillus subtilis
Ollinger, J., Song, K.-B., Antelmann, H., Hecker, M., & Helmann, J. D. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.10.3664-3673.2006 · Cited by 208 · see citing works
Ejrnæs, K. (2011) · PubMed · Cited by 207 · see citing works
Physiological Functions of Bacterial “Multidrug” Efflux Pumps
Henderson, P. J. F., Maher, C., Elbourne, L. D. H., Eijkelkamp, B. A., Paulsen, I. T., & Hassan, K. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01226 · Cited by 203 · see citing works
Anthrax pathogen evades the mammalian immune system through stealth siderophore production
Abergel, R. J., Wilson, M. K., Arceneaux, J. E. L., Hoette, T. M., Strong, R. K., Byers, B. R., & Raymond, K. N. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607055103 · Cited by 198 · see citing works
Self-citationIn Vitro Characterization of Salmochelin and Enterobactin Trilactone Hydrolases IroD, IroE, and Fes
Lin, H., Fischbach, M. A., Liu, D. R., & Walsh, C. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0522027 · Cited by 197 · see citing works
Genome-Wide Screening of Genes Required for Swarming Motility inEscherichia coliK-12
Inoue, T., Shingaki, R., Hirose, S., Waki, K., Mori, H., & Fukui, K. (2006) · Journal of Bacteriology · doi:10.1128/jb.01294-06 · Cited by 197 · see citing works
Gillich, T., Benetti, E. M., Rakhmatullina, E., Konradi, R., Li, W., Zhang, A., Schlüter, A. D., & Textor, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja202760x · Cited by 196 · see citing works
The evolution of siderophore production as a competitive trait
Niehus, R., Picot, A., Oliveira, N. M., Mitri, S., & Foster, K. R. (2017) · Evolution · doi:10.1111/evo.13230 · Cited by 189 · see citing works
The structure of salmochelins: C-glucosylated enterobactins of Salmonella enterica §
Bister, B., Bischoff, D., NICHOLSON, G. J., Valdebenito, M., Schneider, K., Winkelmann, G., Hantke, K., & Süßmuth, R. D. (2004) · BioMetals · doi:10.1023/b:biom.0000029432.69418.6a · Cited by 188 · see citing works
Strzepek, R. F., Maldonado, M. T., Hunter, K. A., Frew, R. D., & Boyd, P. W. (2011) · Limnology and Oceanography · doi:10.4319/lo.2011.56.6.1983 · Cited by 187 · see citing works
Enterococcal Metabolite Cues Facilitate Interspecies Niche Modulation and Polymicrobial Infection
Keogh, D., Tay, W. H., Ho, Y. Y., Dale, J. L., Chen, S., Umashankar, S., Williams, R. B. H., Chen, S. L., Dunny, G. M., & Kline, K. A. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.09.004 · Cited by 184 · see citing works
Bifunctional antimicrobial conjugates and hybrid antimicrobials
Klahn, P., & Brönstrup, M. (2017) · Natural Product Reports · doi:10.1039/c7np00006e · Cited by 182 · see citing works
TolC Is Involved in Enterobactin Efflux across the Outer Membrane of Escherichia coli
Bleuel, C., Große, C., Taudte, N., Scherer, J., Wesenberg, D., Krauss, G.-J., Nies, D. H., & Grass, G. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6701-6707.2005 · Cited by 180 · see citing works
Bacterial heme-transport proteins and their heme-coordination modes
Tong, Y., & Guo, M. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.10.013 · Cited by 176 · see citing works
Gallium-based anti-infectives: targeting microbial iron-uptake mechanisms.
Kelson, A., Carnevali, M., & Truong-Le, V. (2013) · Current opinion in pharmacology (Print) · doi:10.1016/j.coph.2013.07.001 · Cited by 158 · see citing works
Krewulak (2011) · doi:10.1139/o10-141 · Cited by 170 · see citing works
Menyo, M. S., Hawker, C. J., & Waite, J. H. (2013) · Soft Matter · doi:10.1039/c3sm51824h · Cited by 170 · see citing works
<i>In vitro</i> characterization of IroB, a pathogen-associated <i>C</i> -glycosyltransferase
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408463102 · Cited by 169 · see citing works
Zheng, T., & Nolan, E. M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503911p · Cited by 167 · see citing works
Schalk, I. J., & Guillon, L. (2013) · Amino Acids · doi:10.1007/s00726-013-1468-2 · Cited by 167 · see citing works
Microbial siderophore – A boon to agricultural sciences
Ghosh, S. K., Bera, T., & Chakrabarty, A. M. (2020) · Biological Control · doi:10.1016/j.biocontrol.2020.104214 · Cited by 167 · see citing works
Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides
Ongpipattanakul, C., Desormeaux, E. K., DiCaprio, A. J., van der Donk, W. A., Mitchell, D. A., & Nair, S. K. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00210 · Cited by 165 · see citing works
Biological inorganic chemistry at the beginning of the 21st century
Gray, H. B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730378100 · Cited by 161 · see citing works
The role of iron in host–microbiota crosstalk and its effects on systemic glucose metabolism
Mayneris‐Perxachs, J., Moreno‐Navarrete, J. M., & Fernández‐Real, J. M. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00721-3 · Cited by 158 · see citing works
Expression of Virulence Factors by Staphylococcus aureus Grown in Serum
Oogai, Y., Matsuo, M., Hashimoto, M., Kato, F., Sugai, M., & Komatsuzawa, H. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.05316-11 · Cited by 155 · see citing works
Enzyme Promiscuity: Engine of Evolutionary Innovation
Pandya, C., Farelli, J. D., Dunaway‐Mariano, D., & Allen, K. N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.572990 · Cited by 155 · see citing works
Russo, T. A., Shon, A. S., Beanan, J. M., Olson, R., MacDonald, U., Pomakov, A. O., & Visitacion, M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026734 · Cited by 153 · see citing works
Schalk, I. J., Mislin, G. L. A., & Brillet, K. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394390-3.00002-1 · Cited by 153 · see citing works
A Review of Pseudomonas aeruginosa Metallophores: Pyoverdine, Pyochelin and Pseudopaline
Ghssein, G., & Ezzeddine, Z. (2022) · Biology · doi:10.3390/biology11121711 · Cited by 152 · see citing works
Klebba, P. E., Newton, S. M. C., Six, D. A., Kumar, A., Yang, T., Nairn, B. L., Munger, C., & Chakravorty, S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01005 · Cited by 150 · see citing works
Ji, C. Y., Miller, P. A., & Miller, M. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303446w · Cited by 150 · see citing works
Chen, S., Qi, G., Luo, T., Zhang, H., Jiang, Q., Wang, R., & Zhao, X. (2018) · Land Degradation and Development · doi:10.1002/ldr.3167 · Cited by 148 · see citing works
Goltsman, D. S. A., Sun, C. L., Proctor, D. M., DiGiulio, D. B., Robaczewska, A., Thomas, B. C., Shaw, G. M., Stevenson, D. K., Holmes, S., Banfield, J. F., et al. (2018) · Genome Research · doi:10.1101/gr.236000.118 · Cited by 148 · see citing works
Marcelletti, S., Ferrante, P., Petriccione, M., Firrao, G., & Scortichini, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027297 · Cited by 147 · see citing works
Sundlov, J. A., Shi, C., Wilson, D. J., Aldrich, C. C., & Gulick, A. M. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.11.013 · Cited by 146 · see citing works
Gao, Q., Wang, X., Xu, H., Xu, Y., Ling, J., Zhang, D., Gao, S., & Liu, X. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-143 · Cited by 146 · see citing works
Neumann, W., Sassone‐Corsi, M., Raffatellu, M., & Nolan, E. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b01042 · Cited by 144 · see citing works
The ins and outs of siderophore mediated iron uptake by extra-intestinal pathogenic Escherichia coli
Garénaux, A., Caza, M., & Dozois, C. M. (2011) · Veterinary Microbiology · doi:10.1016/j.vetmic.2011.05.023 · Cited by 141 · see citing works
- 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
- Health Sciences › Medicine › Pharmacology › 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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