A much improved synthesis of the siderophore enterobactin

Ramirez, Robert J.A.; Karamanukyan, Levon; Ortiz, Steven M.; Gutiérrez, Carlos Gutièrrez

doi:10.1016/s0040-4039(96)02452-5

Cited by 32 publications

(38 citation statements)

References 19 publications

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“…42 Deprotonation and metalation of a 1:1 mixture of enterobactin and enantioenterobactin provided the potassium salts of the ferric complexes. 43 Salt metathesis with (AsPh 4 )Cl afforded (AsPh 4 ) 3 [Fe(DL-ent)] as a deep red microcrystalline solid.…”

Section: Resultsmentioning

confidence: 99%

Determination of the Molecular Structures of Ferric Enterobactin and Ferric Enantioenterobactin Using Racemic Crystallography

Johnstone

Nolan

2017

J. Am. Chem. Soc.

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Enterobactin is a secondary metabolite produced by Enterobacteriaceae for acquiring iron, an essential metal nutrient. The biosynthesis and utilization of enterobactin permits many Gram-negative bacteria to thrive in environments where low soluble iron concentrations would otherwise preclude survival. Despite extensive work carried out on this celebrated molecule since its discovery over 40 years ago, the ferric enterobactin complex has eluded crystallographic structural characterization. We report the successful growth of single crystals containing ferric enterobactin using racemic crystallization, a method that involves cocrystallization of a chiral molecule with its mirror image. The structures of ferric enterobactin and ferric enantioenterobactin obtained in this work provide a definitive assignment of the stereochemistry at the metal center and reveal secondary coordination sphere interactions. The structures were employed in computational investigations of the interactions of these complexes with two enterobactin-binding proteins, which illuminate the influence of metal-centered chirality on these interactions. This work highlights the utility of small-molecule racemic crystallography for obtaining elusive structures of coordination complexes.

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Section: Resultsmentioning

confidence: 99%

Determination of the Molecular Structures of Ferric Enterobactin and Ferric Enantioenterobactin Using Racemic Crystallography

Johnstone

Nolan

2017

J. Am. Chem. Soc.

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“…Ent was synthesized following a literature procedure, 75 MGE 2 and DGE 3 were prepared from Ent using MceC and IroB as described for MGE-PEG 3 -N 3 12 and DGE-PEG 3 -N 3 13 . Stock solutions of (Glc)Ent 1–3 were prepared in DMSO and stored at –20 °C.…”

Section: Methodsmentioning

confidence: 99%

Targeting virulence: salmochelin modification tunes the antibacterial activity spectrum of β-lactams for pathogen-selective killing of Escherichia coli

2015

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“…Synthetic enterobactin was provided by Carlos Gutierrez (41). All of the other compounds and reagents used in these studies were of American Chemical Society reagent grade or better and were used without further purification.…”

Section: Methodsmentioning

confidence: 99%

Oxidation of Phenolate Siderophores by the Multicopper Oxidase Encoded by the Escherichia coli yacK Gene

et al. 2001

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A gene (yacK) encoding a putative multicopper oxidase (MCO) was cloned from Escherichia coli, and the expressed enzyme was demonstrated to exhibit phenoloxidase and ferroxidase activities. The purified protein contained six copper atoms per polypeptide chain and displayed optical and electron paramagnetic resonance (EPR) spectra consistent with the presence of type 1, type 2, and type 3 copper centers. The strong optical A 610 (⌭ 610 ‫؍‬ 10,890 M ؊1 cm ؊1) and copper stoichiometry were taken as evidence that, similar to ceruloplasmin, the enzyme likely contains multiple type 1 copper centers. The addition of copper led to immediate and reversible changes in the optical and EPR spectra of the protein, as well as decreased thermal stability of the enzyme. Copper addition also stimulated both the phenoloxidase and ferroxidase activities of the enzyme, but the other metals tested had no effect. In the presence of added copper, the enzyme displayed significant activity against two of the phenolate siderophores utilized by E. coli for iron uptake, 2,3-dihydroxybenzoate and enterobactin, as well as 3-hydroxyanthranilate, an iron siderophore utilized by Saccharomyces cerevisiae. Oxidation of enterobactin produced a colored precipitate suggestive of the polymerization reactions that characterize microbial melanization processes. As oxidation should render the phenolate siderophores incapable of binding iron, yacK MCO activity could influence levels of free iron in the periplasm in response to copper concentration. This mechanism may explain, in part, how yacK MCO moderates the sensitivity of E. coli to copper.

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A much improved synthesis of the siderophore enterobactin

Cited by 32 publications

References 19 publications

Determination of the Molecular Structures of Ferric Enterobactin and Ferric Enantioenterobactin Using Racemic Crystallography

Determination of the Molecular Structures of Ferric Enterobactin and Ferric Enantioenterobactin Using Racemic Crystallography

Targeting virulence: salmochelin modification tunes the antibacterial activity spectrum of β-lactams for pathogen-selective killing of Escherichia coli

Oxidation of Phenolate Siderophores by the Multicopper Oxidase Encoded by the Escherichia coli yacK Gene

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