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STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS
Abstract
Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundamental life processes. Owing to their remarkable structural plasticity and versatile chemical/electronic features [Fe-S] clusters participate in electron transfer, substrate binding/activation, iron/sulfur storage, regulation of gene expression, and enzyme activity. Formation of intracellular [Fe-S] clusters does not occur spontaneously but requires a complex biosynthetic machinery. Three different types of [Fe-S] cluster biosynthetic systems have been discovered, and all of them are mechanistically unified by the requirement for a cysteine desulfurase and the participation of an [Fe-S] cluster scaffolding protein. Important mechanistic questions related to [Fe-S] cluster biosynthesis involve the molecular details of how [Fe-S] clusters are assembled on scaffold proteins, how [Fe-S] clusters are transferred from scaffolds to target proteins, how various accessory proteins participate in [Fe-S] protein maturation, and how the biosynthetic process is regulated.
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“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 Johnson et al., 2005
In the citing paper
“iron can act alone or in iron–sulfur clusters as a prosthetic moiety for members of the oxidoreductase, nitrogenase, hydrogenase, dehydrogenase, and hydratase enzyme families [7–12].”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [11]
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“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 a…”
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Emerging critical roles of Fe–S clusters in DNA replication and repair
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“Fe-S clusters are best known for their activities in oxidation-reduction reactions of mitochondrial electron transport, catalysis by aconitase, generation of radicals by SAMdependent enzymes, and sulfur donors in biosynthesis [22].”
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BackgroundLocalization and functionality of microsporidian iron–sulphur cluster assembly proteins
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Genetic Screen for Cell Fitness in High or Low Oxygen Highlights Mitochondrial and Lipid Metabolism
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“For example, it is known that Fe-S clusters can form spontaneously under anaerobic conditions, but in the presence of oxygen, require enzymatic synthesis (Imlay, 2006; Johnson et al., 2005).”
Essential role of Isd11 in mitochondrial iron–sulfur cluster synthesis on Isu scaffold proteins
Wiedemann, N., Urzica, E. I., Guiard, B., Müller, H., Lohaus, C., Meyer, H. E., Ryan, M. T., Meisinger, C., Mühlenhoff, U., Lill, R., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600906 · Cited by 224
“…machinery contain homologs/correlates in the bacterial ISC, NIF and SUF systems for Fe/S cluster biogenesis, while the majority of essential components of the protein import machinery are specific for eukaryotic cells (Pfanner et al, 2004; Johnson et al, 2005; Lill and Mühlenhoff, 2005).”
BackgroundStructure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex
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“The biogenesis of Fe-S clusters have been studied extensively in bacteria, and the mitochondria and plastids of eukaryotes (Frazzon and Dean, 2003; Johnson et al., 2005; Lill and Mühlenhoff, 2005).”
BackgroundMaio, N., & Rouault, T. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.009 · Cited by 222
“It binds target proteins that contain the LYR motif [Fe-S] cluster transfer SIL1 (BAP) Mge1 Nucleotide exchange factor [Fe-S] cluster transfer GLRX5 Grx5 Intermediate carrier [Fe-S] cluster transfer- late acting factor ISCA1 Isa1 [Fe4-S4] assembly [Fe-S] cluster transfer- late acting factor ISCA2 Isa2 [Fe4-S4] assembl…”
BackgroundInfluentialDiscovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis
Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 218
“…selected ISCA1 (yeast ISA1) and C1orf69 (yeast IBA57), which are known to participate in the maturation of Fe-S clusters essential for the activity of a specific subset of mitochondria proteins (Gelling et al., 2008; Johnson et al., 2005), but have not been directly implicated in heme biosynthesis.”
Sheftel, A. D., Wilbrecht, C., Stehling, O., Niggemeyer, B., Elsässer, H., Mühlenhoff, U., & Lill, R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0772 · Cited by 213
“Among other components of Fe/S protein assembly, the isc and suf operons of bacteria encode the so-called A-type iron–sulfur cluster (ISC) proteins IscA and SufA, respectively, which are involved in the maturation of bacterial [4Fe-4S] proteins (Johnson et al., 2005; Tan et al., 2009).”
BackgroundAnalytical measurement of discrete hydrogen sulfide pools in biological specimens
Shen, X., Peter, E. A., Bir, S., Wang, R., & Kevil, C. G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.007 · Cited by 214
“Acid-labile sulfide, the other major pool, consists of sulfur present in the iron–sulfur clusters contained in iron–sulfur proteins (nonheme), which are ubiquitous in living organisms and include a variety of proteins and enzymes including rubredoxins, ferredoxins, aconitase, and succinate dehydrogenase [10,12].”
BackgroundClass I Ribonucleotide Reductases: Metallocofactor Assembly and Repair In Vitro and In Vivo
Cotruvo, J. A., & Stubbe, J. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061408-095817 · Cited by 219
“Pioneering studies of the Dean group (2), followed by work from many labs, have contributed to our understanding of iron-sulfur (FeS) cluster biosynthesis and the complex machinery required (reviewed in Reference 6).”
BackgroundBramley, R. G. V., Ouzman, J., & Boss, P. K. (2011) · Australian Journal of Grape and Wine Research · doi:10.1111/j.1755-0238.2011.00136.x · Cited by 211
Glutaredoxins: roles in iron homeostasis
Rouhier, N., Couturier, J., Johnson, M. K., & Jacquot, J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.08.005 · Cited by 216
Biological chemistry of hydrogen sulfide and persulfides
Cuevasanta, E., Möller, M. N., & Álvarez, B. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.09.018 · Cited by 208
Crack, J. C., Green, J. D., THOMSON, A. J., & Brun, N. E. L. (2014) · Accounts of Chemical Research · doi:10.1021/ar5002507 · Cited by 204
Wen, X., Bai, P., Luo, B., Zheng, S., & Chen, C. (2018) · Corrosion Science · doi:10.1016/j.corsci.2018.05.002 · Cited by 203
Iron–sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
Fontecave, M., & de Choudens, S. O. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.12.014 · Cited by 215
Mammalian iron-sulphur proteins: novel insights into biogenesis and function
Rouault, T. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3909 · Cited by 201
Iron–sulfur proteins in health and disease
Sheftel, A. D., Stehling, O., & Lill, R. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.12.006 · Cited by 208
Cobalt Stress in Escherichia coli
Ranquet, C., de Choudens, S. O., Loiseau, L., Barras, F., & Fontecave, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702519200 · Cited by 199
Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme
Zhang, Y., Zhu, X., Torelli, A. T., Lee, M., Dzikovski, B. G., Koralewski, R. M., Wang, E., Freed, J. H., Krebs, C., Ealick, S. E., et al. (2010) · Nature · doi:10.1038/nature09138 · Cited by 204
“The Fe-S cluster assembly pathways in bacteria and mitochondria of eukaryotes are known to involve J domain-containing co-chaperone proteins, such as bacterial HscB and yeast JAC1 37 , 38 , that are similar to DPH4.”
Ali, V., & Nozaki, T. (2007) · Clinical Microbiology Reviews · doi:10.1128/cmr.00019-06 · Cited by 200
“Fe-S clusters have various important functions, including oxidative phosphorylation, electron transfer, and regulation of gene expression and of enzyme activities including substrate binding and activation, sulfur donation, and iron storage (27, 152).”
BackgroundThe diverse roles of J-proteins, the obligate Hsp70 co-chaperone
Craig, E. A., Huang, P., Aron, R., & Andrew, A. J. (2006) · Springer eBooks · doi:10.1007/s10254-005-0001-0 · Cited by 198
“Both eukaryotes and prokaryotes have specialized systems for the assembly of Fe-S centers, an essential prosthetic group for certain proteins ( Johnson et al. 2005; Lill and Muhlenhoff 2005).”
BackgroundSingh, A., Guidry, L., Narasimhulu, K. V., Mai, D., Trombley, J., Redding, K. E., Giles, G. I., Lancaster, J. R., & Steyn, A. J. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700490104 · Cited by 194
The role of iron in mitochondrial function
Levi, S., & Rovida, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.008 · Cited by 202
Iron-Sulfur (Fe/S) Protein Biogenesis: Phylogenomic and Genetic Studies of A-Type Carriers
Vinella, D., Brochier‐Armanet, C., Loiseau, L., Talla, E., & Barras, F. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000497 · Cited by 191
“sufA iscA Conditional Lethality Is Most Likely Due to Insufficient Maturation of IPP Synthesizing Enzymes IspG/H The iscA and sufA single mutants have repeatedly been found to cause marginal defects [5,6].”
BackgroundTah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis
Netz, D. J. A., Stümpfig, M., Doré, C., Mühlenhoff, U., Pierik, A. J., & Lill, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.432 · Cited by 189
“432" language="eng" relation="no"> Iron-sulfur clusters (Fe-S) are inorganic cofactors of proteins involved in a multitude of essential cellular processes such as electron transfer, enzymatic catalysis, gene regulation, ribosome synthesis, tRNA modification, and DNA replication and repai”
BackgroundThe iron-sulfur cluster assembly machineries in plants: current knowledge and open questions
Couturier, J., Touraine, B., Briat, J., Gaymard, F., & Rouhier, N. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00259 · Cited by 189
Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation
Vickery, L. E., & Cupp‐Vickery, J. R. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701322298 · Cited by 188
“…of genetic and biochemical approaches have led to the identification of three types of systems involved in [FeS]-cluster assembly and maturation, and each contains a group of highly specialized proteins (see reviews by Johnson et al., 2005; Mühlenhoff and Lill, 2006; Rouault and Tong, 2005).”
BackgroundFBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster
Wang, H., Shi, H., Rajan, M., Canarie, E. R., Hong, S., Simoneschi, D., Pagano, M., Bush, M. F., Stoll, S., Leibold, E. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.011 · Cited by 184
“Iron-sulfur clusters have long been documented to play critical roles in a variety of biological regulatory mechanisms by sensing the levels of different physiological factors (Johnson et al., 2005; Lill, 2009; Rouault, 2015).”
BackgroundPrischi, F., Konarev, P. V., Iannuzzi, C., Pastore, C., Adinolfi, S., Martin, S. R., Svergun, D. I., & Pastore, A. (2010) · Nature Communications · doi:10.1038/ncomms1097 · Cited by 186
“7), which catalyses the reaction that converts l-cysteine into alanine and a highly reactive sulphide, and the scaffold protein on which the cluster is transiently forme”
BackgroundFluorescent probes for ferroptosis bioimaging: advances, challenges, and prospects
Yin, J., Zhan, J., Hu, Q., Huang, S., & Lin, W. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00454b · Cited by 183
A review of the effects of iron compounds on methanogenesis in anaerobic environments
Baek, G., Kim, J., & Lee, C. (2019) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2019.109282 · Cited by 190
SufE Transfers Sulfur from SufS to SufB for Iron-Sulfur Cluster Assembly
Layer, G., Gaddam, S. A., Ayala-Castro, C. N., de Choudens, S. O., Lascoux, D., Fontecave, M., & Outten, F. W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608555200 · Cited by 182
Genetic Architecture of Intrinsic Antibiotic Susceptibility
Girgis, H. S., Hottes, A. K., & Tavazoie, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005629 · Cited by 179
“The media used lacks cysteine, the sulfur donor for iron-sulfur center synthesis [88], so disruption of cysteine biosynthesis should reduce the availability of sulfur for iron-sulfur centers.”
BackgroundWebert, H., Freibert, S., Gallo, A., Heidenreich, T., Linne, U., Amlacher, S., Hurt, E., Mühlenhoff, U., Banci, L., & Lill, R. (2014) · Nature Communications · doi:10.1038/ncomms6013 · Cited by 176
Metadata
- Authors
- Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K.
- Affiliations
- Virginia Tech (US)
- University of Georgia (US)
- ORCID
- Dean, Dennis R.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2005-06-01
- Volume
- 74
- Issue
- 1
- Pages
- 247-281
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2116472408
- Cited by
- 1,438
- References
- 209
- Citations by year
- 2026: 48 · 2025: 68 · 2024: 57 · 2023: 62 · 2022: 75 · 2021: 94 · 2020: 64 · 2019: 67 · 2018: 65 · 2017: 72 · 2016: 64 · 2015: 63 · 2014: 73 · 2013: 69 · 2012: 74
- FWCI
- 7.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM62524)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Inorganic Chemistry and Materials
- Keywords
- iron-sulfur clusters, Fe-S cluster biosynthesis, cysteine desulfurase, cluster assembly, protein maturation, electron transfer, prosthetic groups, gene expression regulation, enzyme activity
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Carrier Proteins, Escherichia coli, Genes, Bacterial, Iron-Sulfur Proteins, Molecular Sequence Data, Nitrogenase, Protein Processing, Post-Translational, Sequence Homology, Amino Acid, Escherichia coli Proteins
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