Models for the bacterial iron-transport chelate enterochelin

  title={Models for the bacterial iron-transport chelate enterochelin},
  author={Bryan F. Anderson and David A. Buckingham and Glen B. Robertson and John Webb and Keith S. Murray and Paul E. Clark},
MICROBIAL iron-transport compounds, or siderochromes are of two general structural types, the phenolates and the hydroxa-mates1,2. X-ray studies of several of the latter, for example, ferrichrome A (ref. 3), ferrioxamine E (ref. 4) and myco-bactin P (ref. 5), establish the anion of hydroxamic acid (−N(O−)CO−) as the dominant metal-binding moiety, with discrete, neutral [FeO6] (refs 3 and 4) or [FeO5N] (ref. 5) units being involved. No similar structural data are at present available, however… 
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The Competition between Enterobactin and Glutathione for Iron
The competition for iron between thiol and catechol compounds is described. At pH values <7.0, both mercaptoethanol and glutathione are able to completely remove iron from catechol. Although it is
Iron(III) complexes of chrysobactin, the siderophore ofErwinia chrysanthemi
The phytopathogenic bacteriumErwinia chrysanthemi produces the monocatecholate siderophore chrysobactin under conditions of iron deprivation, which is unable to provide full 1:1 coordination of Fe(III), and the stoichiometry in aqueous solution is a variable dependent on pH and metal/ligand ratio.
Infrared multiphoton dissociation of the siderophore enterobactin and its Fe(III) complex. Influence of Fe(III) binding on dissociation kinetics and relative energetics
The results suggest that at pH = 3.5, Fe(III) interacts with only two of the three serine groups, which is valuable for the characterization of novel siderophores as well as their associated metabolites and synthetic analogues.
Ferric enterobactin transport system in Escherichia coli K-12. Extraction, assay, and specificity of the outer membrane receptor.
An outer membrane preparation from cells of Escherichia coli K-12 grown in low iron medium was found to retain ferric enterobactin binding activity following solubilization in a Tris-HCl, Na2EDTA
Electronic and resonance Raman spectra of iron(III) complexes of enterobactin, catechol, and N-methyl-2,3-dihydroxybenzamide.
The spectral signatures of the enterobactin and MDHB complexes are virtually identical and differ from those of the catechol complex in ways that reflect the influence of the amide group on the electronic structure.
Novel method to examine the formation of unstable 2:1 and 3:1 complexes of catecholamines and iron(III)☆
Abstract The formation of the 2:1 and 3:1 complexes of the catecholamines, epinephrine and norephinephrine, as well as the less easily oxidized catechol, and iron(III) was studied in a physiological
Crystal and molecular structure of piperidinium μ-acetato-di-μ-1,2-benzenediolato-bis-1,2-benzenediolatoferrate(III), (C5H12N)3 [(CH3COO){Fe(C6H4O2)2}2]: a compound of relevance to the 2Fe-active site of the respiratory protein hemerythrin ☆
Abstract The title compound is readily prepared as chunky purple-black crystals with the space group P 4 . The crystal structure was determined to a conventional R value of 0.088. The two FeO6
A Bioinorganic View of the Biological Mineralization of Iron
A variety of mineralized iron deposits is now known to occur in a range of living organisms, extending from microorganisms to higher vertebrates. Minerals reported include magnetite, maghemite,
Protein binding of iron in blood plasma of the ascidian Herdmania momus
Iron-binding in the plasma of blood of the ascidian Herdmania momus var.
Ferric nitrilotriacetate Fe(NTA) binds 3,5-di-t-butyl- catechol DBcatH2 to form a ternary complex, [Fe(NTA)(DBcat)]2-. Upon exposure to 02, dioxygenation leads to ring cleavage of the catechol,


Publisher Summary This chapter focuses on iron transport in the enteric bacteria. It seems very likely that the transport of ferric iron into bacteria must involve a chelator to solubilize the
Electronic state of iron in enterobactin using Mössbauer spectroscopy
Well‐resolved paramagnetic hyperfine structure is observed in the Mossbauer spectra of 57Fe complexed by enterobactin, an iron transport compound found in many enteric bacteria. Spectra were observed
The structure of enterochelin and related 2,3-dihydroxy-N-benzoylserine conjugates from Escherichia coli.
Five compounds, each containing 2,3-dihydroxybenzoic acid and serine, have been isolated from culture media of Escherichia coli and Aerobacter aerogenes grown under conditions of iron deficiency.
The crystal structure of ferrimycobactin P, a growth factor for the Mycobacteria.
  • E. Hough, D. Rogers
  • Chemistry, Medicine
    Biochemical and biophysical research communications
  • 1974
Abstract An X-ray study of the crystal structure of ferrimycobactin P has confirmed in detail Snow's structure and absolute stereochemistry for mycobactin P and has identified the iron coordination
Mössbauer effect and susceptibility studies of a dimeric Schiff-base iron(III) adduct
Variable-temperature susceptibility and Mossabauer effect measurements of the nitromethane adduct Fe(salen) Cl,-½MeNO2 are reported. The susceptibility from 13 to 300°K is well explained by the
The crystal structure of ferrioxamine E.