Enterochelin hydrolysis and iron metabolism in Escherichia coli

Ig, O'Brien; Gb, Cox; Gibson, F.

doi:10.1016/0304-4165(71)90274-1

Cited by 133 publications

(82 citation statements)

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“…As shown in Fig. 7, the viuB promoter region has an area of dyad (8,9,12,18 (5,20,26,27 The identification of a second gene in the vibriobactin uptake apparatus adjacent to viuA, the ferric vibriobactin outer membrane receptor, suggests that other genes involved in vibriobactin biosynthesis and uptake may be clustered in this region. A large DNA fragment downstream of viuB has been recovered from the 0395 chromosome and is being examined.…”

Section: Resultsmentioning

confidence: 99%

“…The E. coli siderophore, enterobactin, has been extensively studied; the biosynthetic steps needed for its synthesis have been determined, and the gene cluster containing the biosynthetic and uptake genes has been defined (11,27). The enterobactin genes span approximately 22 kbp at min 13 on the E. coli chromosome; this large cluster contains six biosynthetic (ent) genes and six genes involved in transport, including fepA, which encodes the outer membrane receptor; fepB, encoding a periplasmic binding protein; and fepC, fepD, iron from the ferric enterobactin complex after entry into the cytoplasm (5,20,26,27). These genes involved in iron uptake are themselves regulated by iron, with increased amounts of siderophore and outer membrane receptor produced under low-iron conditions (11,(25)(26)(27).…”

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confidence: 99%

“…The enterobactin genes span approximately 22 kbp at min 13 on the E. coli chromosome; this large cluster contains six biosynthetic (ent) genes and six genes involved in transport, including fepA, which encodes the outer membrane receptor; fepB, encoding a periplasmic binding protein; and fepC, fepD, iron from the ferric enterobactin complex after entry into the cytoplasm (5,20,26,27). These genes involved in iron uptake are themselves regulated by iron, with increased amounts of siderophore and outer membrane receptor produced under low-iron conditions (11,(25)(26)(27). Iron regulation of the genes in the enterobactin gene cluster is under the control of the protein product of the fur gene, which represses gene transcription in high-iron conditions (2,8,9,12,13,17,18).…”

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Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae

Butterton

Calderwood

1994

J Bacteriol

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Several distinct methods of scavenging iron have been characterized for the human pathogen Vibrio cholerae. Iron, an essential element for bacterial growth and survival (6, 10, 11), is not freely available under aerobic conditions; bacteria need either to extract iron from insoluble mineral complexes or to compete with the host's own strategies for sequestering iron from invading organisms. Many bacteria have developed siderophores-low-molecular-weight iron chelators-which effectively compete with human iron-binding proteins, such as lactoferrin and transferrin (11,24,30), while others have evolved outer membrane protein receptors that can bind human transferrin, lactoferrin, or hemin directly to obtain iron (3,33,34). V cholerae produces a siderophore, vibriobactin (16), but mutants defective in vibriobactin production or utilization can survive either by resorting to a system that uses ferric citrate (36) or by using hemin or hemoglobin in a siderophore-independent mechanism (38).The V cholerae phenolate type siderophore, vibriobactin, is similar in structure to the Escherichia coli siderophore, enterobactin, and the Agrobacterium tumefaciens siderophore, agrobactin (16). The E. coli siderophore, enterobactin, has been extensively studied; the biosynthetic steps needed for its synthesis have been determined, and the gene cluster containing the biosynthetic and uptake genes has been defined (11,27). The enterobactin genes span approximately 22 kbp at min 13 on the E. coli chromosome; this large cluster contains six biosynthetic (ent) genes and six genes involved in transport, including fepA, which encodes the outer membrane receptor; fepB, encoding a periplasmic binding protein; and fepC, fepD,

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Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae

Butterton

Calderwood

1994

J Bacteriol

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“…Furthermore, the bacteria are unable to use the cleavage product, 2,3-dihydroxybenzoylserine, as a substrate for enterobactin synthesis, which occurs instead via condensation of 2,3-dihydroxybenzoic acid and serine. (12). Thus each molecule of enterobactin yields one iron atom to the cell and then is destroyed.…”

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confidence: 99%

“…Thus one siderophore molecule can shuttle more than one iron ion into the organism. By contrast, the cyclic triester linkages of ferric enterobactin are cleaved by an esterase specific for the ferric complex (12,13). Esterase-deficient mutants are colored pink due to intracellular ferri-enterobactin (in contrast to the white cells of the parent strain) but grow poorly under iron stress, establishing that esterase activity is vital to enterobactin-mediated transport.…”

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Siderophore electrochemistry: relation to intracellular iron release mechanism.

Cooper¹,

McArdle²,

Raymond³

1978

Proc. Natl. Acad. Sci. U.S.A.

126

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Previous studies have shown that there is a major difference between the iron release mechanism of enterobactin, a catechol-based siderophore, and that of the hydroxamate-based siderophores such as ferrichrome. For ferric enterobactin there is an esterase that hydrolyzes the ligand during iron release. In contrast, iron is released by the hydroxamate-based siderophores and the ligands are reused in subsequent iron transport. It has been suggested that release of iron by hydroxamates occurs by reduction to the ferrous complex, a process that does not occur for ferric enterobactin. Cyclic vo tammograms of ferrichrome A and ferrioxamine B exhibit reversible one-electron waves with pH-independent formal potentials (Ef vs. the normal hydrogen electrode) -446 and -454 mV, respectively, within the range of physiological reductants. Ferric enterobactin also shows a reversible one-electron wave (at pH > 10) with Ef = -986 mV vs. the normal hydrogen electrode. From the pH dependence of this potential we estimate a reduction potential of -750 mV at pH 7. In sharp contrast to the value for the ferric hydroxamates, this value is well below the range of physiological reducing agents. The results demonstrate that the observed hydrolysis of enterobactin is a necessary prerequisite to in vivo release of iron from the siderophore via ferric ion reduction.

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Natural and Biomimetic Hydroxamic Acid Based Siderophores

Shanzer

Felder

Barda

2010

Patai's Chemistry of Functional Groups

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Introduction Physical and Chemical Properties of Hydroxamate‐Based Siderophores Iron Metabolism Biomimetic Chemistry Natural and Biomimetic Hydroxamic Acid Based Siderophores Siderophore Conjugates Biomimetic Siderophores in Health and Disease Acknowledgments

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Enterochelin hydrolysis and iron metabolism in Escherichia coli

Cited by 133 publications

References 12 publications

Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae

Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae

Siderophore electrochemistry: relation to intracellular iron release mechanism.

Natural and Biomimetic Hydroxamic Acid Based Siderophores

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