Spectroscopic Observations of Ferric Enterobactin Transport

Cao, Zhenghua; Warfel, Paul; Newton, Salete M.C.; Klebba, Phillip E.

doi:10.1074/jbc.m210360200

Cited by 39Bacterial Genetics and BiotechnologyDrug Transport and Resistance MechanismsEscherichia coli research studies

Spectroscopic Observations of Ferric Enterobactin Transport

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Cao, Zhenghua, Warfel, Paul, Newton, Salete M.C., Klebba, Phillip E.·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.m210360200

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Abstract

We characterized the uptake of ferric enterobactin (FeEnt), the native Escherichia coli ferric siderophore, through its cognate outer membrane receptor protein, FepA, using a site-directed fluorescence methodology. The experiments first defined locations in FepA that were accessible to covalent modification with fluorescein maleimide (FM) in vivo; among 10 sites that we tested by substituting single Cys residues, FM labeled W101C, S271C, F329C, and S397C, and all these exist within surface-exposed loops of the outer membrane protein. FeEnt normally adsorbed to the fluoresceinated S271C and S397C mutant FepA proteins in vivo, which we observed as quenching of fluorescence intensity, but the ferric siderophore did not bind to the FM-modified derivatives of W101C or F329C. These in vivo fluorescence determinations showed, for the first time, consistency with radioisotopic measurements of the affinity of the FeEnt-FepA interaction; K(d) was 0.2 nm by both methods. Analysis of the FepA mutants with AlexaFluor(680), a fluorescein derivative with red-shifted absorption and emission spectra that do not overlap the absorbance spectrum of FeEnt, refuted the possibility that the fluorescence quenching resulted from resonance energy transfer. These and other data instead indicated that the quenching originated from changes in the environment of the fluor as a result of loop conformational changes during ligand binding and transport. We used the fluorescence system to monitor FeEnt uptake by live bacteria and determined its dependence on ligand concentration, temperature, pH, and carbon sources and its susceptibility to inhibition by the metabolic poisons. Unlike cyanocobalamin transport through the outer membrane, FeEnt uptake was sensitive to inhibitors of electron transport and phosphorylation, in addition to its sensitivity to proton motive force depletion.

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Fluorescently labeled LGP reflect the binding and uptake of their ligands.
“Fluorescently labeled LGP reflect the binding and uptake of their ligands (17,(37)(38)(39).”
From Siderophore-mediated iron acquisition by Klebsiella pneumoniae (2024) · cites this paper as [37]

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Concerted loop motion triggers induced fit of FepA to ferric enterobactin
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Self-citation

Authors: Cao, Z., Warfel, P., Newton, S. M. C., & Klebba, P. E.
Affiliations: University of Oklahoma (US)
Corresponding author: Cao, Zhenghua
Klebba, Phillip E.
ORCID: Newton, Salete M.C.
Klebba, Phillip E.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2003-01
Volume: 278
Issue: 2
Pages: 1022-1028
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m210360200
OpenAlex: W2171899761
Cited by: 39
References: 56
Citations by year: 2025: 1 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 1 · 2017: 3 · 2016: 1 · 2015: 1 · 2014: 4 · 2013: 1 · 2012: 1
FWCI: 2.29
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6491 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (R01GM053836)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
Keywords: FepA, siderophore uptake, Escherichia coli, outer membrane receptor, fluorescence quenching, loop conformational change, ligand binding, electron transport inhibition, proton motive force
MeSH terms: Biological Transport, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Enterobactin, Hydrogen-Ion Concentration, Lipopolysaccharides, Spectrometry, Fluorescence, Temperature, Escherichia coli Proteins

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Spectroscopic Observations of Ferric Enterobactin Transport

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