Mammalian iron-sulphur proteins: novel insights into biogenesis and function
Abstract
Iron-sulphur (Fe-S) clusters are inorganic cofactors that are found in nearly all species and are composed of various combinations of iron and sulphur atoms. Fe-S clusters can accept or donate single electrons to carry out oxidation and reduction reactions and to facilitate electron transport. Many details of how these complex modular structures are assembled and ligated to cellular proteins in the mitochondrial, nuclear and cytosolic compartments of mammalian cells remain unclear. Recent evidence indicates that a Leu-Tyr-Arg (LYR) tripeptide motif found in some Fe-S recipient proteins may facilitate the direct and shielded transfer of Fe-S clusters from a scaffold to client proteins. Fe-S clusters are probably an unrecognized and elusive cofactor of many known proteins.
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IRP1 usually loses its iron-sulfur cluster and aconitase activity and binds IREs with high affinity.
“In this situation, IRP1 usually loses its iron-sulfur cluster and aconitase activity and binds IREs with high affinity [48], [50].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [50]
Defects in Fe-S cluster synthesis cause numerous diseases, primarily neurologic disorders such as Friedreich ataxia and Parkinson disease.
“Defects in this process cause numerous diseases [ 27 , 28 ], primarily neurologic disorders such as Friedreich ataxia and Parkinson disease [ 29 ].”
From Steroidogenic electron-transfer factors and their diseases (2021) · cites this paper as [27]
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- Authors
- Rouault, T. A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Rouault, Tracey A.
- ORCID
- Rouault, Tracey A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-11-26
- Volume
- 16
- Issue
- 1
- Pages
- 45-55
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1964601437
- Cited by
- 201
- References
- 112
- Citations by year
- 2026: 10 · 2025: 16 · 2024: 17 · 2023: 8 · 2022: 12 · 2021: 17 · 2020: 17 · 2019: 20 · 2018: 23 · 2017: 27 · 2016: 19 · 2015: 15
- FWCI
- 0.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Eunice Kennedy Shriver National Institute of Child Health and Human Development
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- iron-sulfur clusters, iron-sulfur proteins, iron-sulfur cluster assembly, electron transfer, mammalian cells, mitochondrial proteins, cytosolic proteins, nuclear proteins
- MeSH terms
- Animals, Electron Transport, Humans, Iron-Sulfur Proteins, Oxidation-Reduction, Amino Acid Motifs
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