The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
Iron–sulfur cluster biogenesis and trafficking in mitochondria
Open accessAbstract
The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular functions, including genome maintenance, protein translation, energy conversion, and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S] clusters and their incorporation into numerous apoproteins. Mechanistic aspects of Fe/S protein biogenesis continue to be elucidated by biochemical and ultrastructural investigations. Here, we review recent developments in the pursuit of constructing a comprehensive model of Fe/S protein assembly in the mitochondrion.
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“Once inside the organelle the iron is incorporated into heme and iron-sulfur (Fe-S) clusters by frataxin and GLRX5 (Glutaredoxin-related protein 5) (Lill, 2009; Braymer and Lill, 2017).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Braymer and Lill, 2017
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Cites
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“These cofactors participate in electron transfer reactions, Lewis acid catalysis, transfer of sulfur atoms, or facilitating structural roles (5, 6).”
BackgroundProtein structure homology modeling using SWISS-MODEL workspace
Bordoli, L., Kiefer, F., Arnold, K., Benkert, P., Battey, J. N. D., & Schwede, T. F. (2008) · Nature Protocols · doi:10.1038/nprot.2008.197 · Cited by 1,233
Chaperone machines for protein folding, unfolding and disaggregation
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Function and biogenesis of iron-sulphur proteins
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Self-citationIron-sulfur proteins: ancient structures, still full of surprises
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Assembly of Iron-Sulfur Clusters
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Structure of mammalian respiratory complex I
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The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 513
Self-citationGrx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
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The Origin and Diversification of Mitochondria
Roger, A. J., Muñoz-Gómez, S. A., & Kamikawa, R. (2017) · Current Biology · doi:10.1016/j.cub.2017.09.015 · Cited by 1,142
Iron metabolism and iron disorders revisited in the hepcidin era
Camaschella, C., Nai, A., & Silvestri, L. (2020) · Haematologica · doi:10.3324/haematol.2019.232124 · Cited by 734
“Biogenesis of Fe/S clusters is a process conserved from yeast to humans: this prosthetic group is essential to proteins involved in genome maintenance, energy conversion, iron regulation and protein translation.(14,15) In erythroblasts >80% iron is directed to mitochondria through a “kiss and run” mechanism between en…”
Multifaceted mitochondria: moving mitochondrial science beyond function and dysfunction
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Iron homeostasis and iron-regulated ROS in cell death, senescence and human diseases
Nakamura, T., Naguro, I., & Ichijo, H. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.06.010 · Cited by 529
Mitochondrial iron–sulfur clusters: Structure, function, and an emerging role in vascular biology
Read, A. D., Bentley, R. E. T., Archer, S. L., & Dunham‐Snary, K. J. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102164 · Cited by 440
Metadata
- Authors
- Braymer, J. J., & Lill, R.
- Affiliations
- Philipps University of Marburg (DE)
- Corresponding author
- Lill, Roland
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2017-08
- Volume
- 292
- Issue
- 31
- Pages
- 12754-12763
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5546016
- OpenAlex
- W2625087901
- Cited by
- 389
- References
- 100
- Citations by year
- 2026: 29 · 2025: 29 · 2024: 32 · 2023: 39 · 2022: 45 · 2021: 40 · 2020: 56 · 2019: 44 · 2018: 57 · 2017: 16
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (Koselleck grant, LI 415/5, SFB 987, SPP 1710, and SPP 1927)
- German-Israeli Foundation for Scientific Research and Development (I-1302-412.13/2015)
- H2020 Marie Skłodowska-Curie Actions (659325)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- iron-sulfur clusters, mitochondrial iron-sulfur proteins, [2Fe-2S] cluster, [4Fe-4S] cluster, cluster assembly, iron-sulfur proteins, genome maintenance, mRNA translation, energy conversion, antiviral response
- MeSH terms
- Frataxin, Acyl Carrier Protein, Adrenodoxin, Animals, Apoenzymes, Humans, Iron-Sulfur Proteins, Mitochondria, Models, Biological, Models, Molecular, Protein Conformation, Species Specificity, Sulfurtransferases, Gene Expression Regulation, Enzymologic, Protein Folding, Protein Transport, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Iron-Binding Proteins, Protein Multimerization
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