Cited by 24Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsHemoglobin structure and function

Iron Binding Site in a Global Regulator in Bacteria–Ferric Uptake Regulator (Fur) Protein: Structure, Mössbauer Properties, and Functional Implication

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Katigbak, Joseph, Zhang, Yong·2012·The Journal of Physical Chemistry Letters

Abstract

Fur protein plays key roles in regulating numerous genes in bacteria and is essential for intracellular iron concentration regulation. However, atomic level pictures of the iron binding site and its functional mechanism remain to be established. Here we present results of the first quantum chemical investigation of various first- and second-shell models and experimental Mössbauer data of E. Coli Fur, including 1) the first robust evidence that site 2 is the Fe binding site with a 3His/2Glu ligand set, being the first case in non-heme proteins, with computed Mössbauer data in excellent accord with experiment; 2) the first discovery of a conservative hydrogen bonding interaction in the iron binding site based on X-ray and homology structures; 3) the first atomic level hypothesis of active site reorganization upon iron concentration increase, triggering the conformational change needed for its function. These results shall facilitate structural and functional studies of Fur family proteins.

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Authors
Katigbak, J., & Zhang, Y.
Affiliations
Stevens Institute of Technology (US)
Corresponding author
Zhang, Yong
Venue
The Journal of Physical Chemistry Letters
Published
2012-11-15
Volume
3
Issue
23
Pages
3503-3508
ISSN
1948-7185 (ISSN-L)
OpenAlex
W2022729414
Cited by
24
References
38
Citations by year
2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 1 · 2016: 2 · 2015: 2 · 2014: 5 · 2013: 2 · 2012: 1
FWCI
1.23
Type
journal article
Language
en
Open access
Locations
  • The Journal of Physical Chemistry Letters (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (R15GM085774)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords
Fur protein, ferric uptake regulator, iron binding sites, Escherichia coli, Mössbauer spectroscopy, quantum chemical calculations, non-heme iron, hydrogen bonding, conformational change, iron regulation, global transcriptional regulator, homology modeling

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