Iron-sulfur proteins: ancient structures, still full of surprises
Abstract
This article is a survey of the properties and functions of Fe-S proteins under the following headings: sulfur and iron; iron-sulfur clusters; evolution of cofactor use; early observations; complex and extended clusters; sulfur exchange and core interconversions; synthesis and biosynthesis of Fe-S clusters; functions of Fe-S clusters: electron transfer, electron delocalization, spin states and magnetism, covalency of sulfur bonds; non-electron transfer functions of Fe-S clusters: substrate binding and catalysis, regulatory and sensing functions.
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Fe-S clusters are ubiquitous inorganic co-factors that contribute to genome integrity, gene regulation, energy production, and immune responses, and are required for numerous biological functions, particularly enzymatic activity.
“Fe-S clusters are ubiquitous, inorganic co-factors that contribute to a wide range of cellular pathways from genome integrity and gene regulation to energy production and immune responses, and are required for numerous biological functions, particularly enzymatic activity (Beinert, 2000; Johnson et al., 2005; Lee et al., 2009; Fuss et al., 2015).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Beinert, 2000
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Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works
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“Coenzyme A itself is a thiol, and life has taken full advantage of the fact that sulfur is equally at home ligated to the transition metals as it is bound to carbon and with itself (Beinert, 2000a, 2000b).”
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- Authors
- Beinert, H.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Beinert, H.
- Venue
- JBIC Journal of Biological Inorganic Chemistry
- Published
- 2000-02
- Volume
- 5
- Issue
- 1
- Pages
- 2-15
- ISSN
- 0949-8257 (ISSN-L)
- 1432-1327
- OpenAlex
- W2073746011
- Cited by
- 667
- References
- 1
- Citations by year
- 2026: 7 · 2025: 25 · 2024: 30 · 2023: 23 · 2022: 30 · 2021: 41 · 2020: 25 · 2019: 20 · 2018: 28 · 2017: 24 · 2016: 25 · 2015: 30 · 2014: 28 · 2013: 40 · 2012: 29
- FWCI
- 28.77
- Type
- journal article
- Language
- en
- Update notices
- erratum (2000-11-06)
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Inorganic Chemistry and Materials
- Keywords
- iron-sulfur proteins, iron-sulfur clusters, electron transfer, electron delocalization, spin states, magnetism, protein evolution
- MeSH terms
- Iron-Sulfur Proteins, Models, Molecular, Evolution, Molecular
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