Iron Binding Site in a Global Regulator in Bacteria–Ferric Uptake Regulator (Fur) Protein: Structure, Mössbauer Properties, and Functional Implication
Open accessAbstract
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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Site 1 is the Fe2+-binding site with a 3His/2Glu ligand set.
“site 1 is the Fe 2+ -binding site with a 3His/2Glu ligand set 36 .”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [36]
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- Authors
- Katigbak, J., & Zhang, Y.
- Affiliations
- Stevens Institute of Technology (US)
- Corresponding author
- Zhang, Yong
- ORCID
- Zhang, Yong
- Venue
- The Journal of Physical Chemistry Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-11-15
- Volume
- 3
- Issue
- 23
- Pages
- 3503-3508
- ISSN
- 1948-7185 (ISSN-L)
- PMC
- PMC3507992
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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