Cited by 1,438Metalloenzymes and iron-sulfur proteinsEnzyme Structure and FunctionInorganic Chemistry and Materials

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STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS

Johnson, Deborah C., Dean, Dennis R., Smith, Archer D., Johnson, Michael K.·2005·Annual Review of Biochemistry

DOI 10.1146/annurev.biochem.74.082803.133518

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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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Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891
DNA Microarray-Mediated Transcriptional Profiling of the Escherichia coli Response to Hydrogen Peroxide
Zheng, M., Wang, X., Templeton, L. J., Smulski, D. R., LaRossa, R. A., & Storz, G. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.15.4562-4570.2001 · Cited by 802
Activated Acetic Acid by Carbon Fixation on (Fe,Ni)S Under Primordial Conditions
Huber, C., & Wächtershäuser, G. (1997) · Science · doi:10.1126/science.276.5310.245 · Cited by 714
The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699
Iron-sulfur proteins: ancient structures, still full of surprises
Beinert, H. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050002 · Cited by 667
Assembly of Iron-Sulfur Clusters
Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 650
Density-Functional Theory of Spin Polarization and Spin Coupling in Iron—Sulfur Clusters
Noodleman, L., & Case, D. A. (1992) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60070-7 · Cited by 620
Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
Tovar, J., León-Ávila, G., Sánchez, L. B., Šuťák, R., Tachezy, J., van der Giezen, M., Hernández, M., Müller, M., & Lucocq, J. M. (2003) · Nature · doi:10.1038/nature01945 · Cited by 609

Show all 209 references

Research works printed but not linked: 4

Johnson MK. 1994. InEncyclopedia of Inorganic Chemistry, ed.RB King, pp.1896–915. Chichester, UK: Wiley
Thauer RK, Schonheit P. 1982. InIron-Sulfur Proteins, ed.TG Spiro, pp.329–41. New York: Wiley
10.1074/jbc.275.12.8283 · DOI
10.1074/jbc.M104067200 · DOI

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“In this reaction, the released sulfur is then transferred into scaffold protein to assemble Fe–S clusters [62], and these clusters have been shown to participate in electron transfer, iron–sulfur storage, regulation of gene expression, photosynthesis, and enzyme activity in all kingdoms of life [63].”
Background
Induction of ferroptosis in head and neck cancer: A novel bridgehead for fighting cancer resilience
Lee, J., & Roh, J. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215854 · Cited by 27
Organic and inorganic mercurials have distinct effects on cellular thiols, metal homeostasis, and Fe-binding proteins in Escherichia coli
LaVoie, S. P., Mapolelo, D. T., Cowart, D. M., Polacco, B. J., Johnson, M. K., Scott, R. A., Miller, S. M., & Summers, A. O. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1303-1 · Cited by 25
ChIP-seq analysis reveals alteration of H3K4 trimethylation occupancy in cancer-related genes by cold atmospheric plasma
Lee, S.-Y., Park, S.-B., Lee, H.-K., Jeong, D., Ham, J., Choi, E. H., & Kim, S. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.004 · Cited by 25
Fosmidomycin, an inhibitor of isoprenoid synthesis, induces persistence in Chlamydia by inhibiting peptidoglycan assembly
Slade, J. A., Brockett, M. R., Singh, R., Liechti, G. W., & Maurelli, A. T. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008078 · Cited by 25
“Upon entry into the bacterial cytoplasm, free iron must be assembled into iron-sulfur clusters and chaperoned to the enzymes that require these cofactors to function [48].”
Background
Effects of Amino Acids on Iron-Silicate Chemical Garden Precipitation
Hooks, M., Webster, P. C., Weber, J. M., Perl, S. M., & Barge, L. M. (2020) · Langmuir · doi:10.1021/acs.langmuir.0c00502 · Cited by 25
Understanding electron transport systems of Streptomyces cytochrome P450
Chun, Y., Shimada, T., Waterman, M. R., & Guengerich, F. P. (2006) · Biochemical Society Transactions · doi:10.1042/bst0341183 · Cited by 25
Transcription of the extended hyp-operon in Nostocsp. strain PCC 7120
Agervald, Å., Stensjö, K., Holmqvist, M. E., & Lindblad, P. C. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-69 · Cited by 25
“How the assembly and maturation process is achieved is not well known, but three different types of (FeS) cluster assembly have been presented with two requirements in common: the need for a (FeS) scaffolding protein, and a cysteine desulphurase which is required to yield elemental sulphur or hydrogen sulphide [12, 18…”
Background
Spin‐Regulated Electron Transfer and Exchange‐Enhanced Reactivity in Fe 4 S 4 ‐Mediated Redox Reaction of the Dph2 Enzyme During the Biosynthesis of Diphthamide
Feng, J., Shaik, S. S., & Wang, B. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202107008 · Cited by 24
The Result of Vitamin C Treatment of Patients with Cancer: Conditions Influencing the Effectiveness
Hunyady, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084380 · Cited by 29
The Specialized Hsp70 (HscA) Interdomain Linker Binds to Its Nucleotide-Binding Domain and Stimulates ATP Hydrolysis in Both cis and trans Configurations
Alderson, T. R., Kim, J. H., Cai, K., Frederick, R. O., Tonelli, M., & Markley, J. L. (2014) · Biochemistry · doi:10.1021/bi5010552 · Cited by 24
Modelling Low‐Potential [Fe4S4] Clusters in Proteins
Koay, M. S. T., Antonkine, M. L., Gärtner, W., & Lubitz, W. (2008) · Chemistry & Biodiversity · doi:10.1002/cbdv.200890145 · Cited by 24
Importance of Hydrogen Bonding in Fine Tuning the [2Fe-2S] Cluster Redox Potential of HydC from Thermotoga maritima
Birrell, J. A., Laurich, C., Reijerse, E. J., Ogata, H., & Lubitz, W. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00341 · Cited by 24
The Escherichia coli BolA Protein IbaG Forms a Histidine-Ligated [2Fe-2S]-Bridged Complex with Grx4
Dlouhy, A. C., Li, H., Albetel, A., Zhang, B., Mapolelo, D. T., Randeniya, S., Holland, A. A., Johnson, M. K., & Outten, C. E. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00812 · Cited by 24
Profiling of sperm gene transcripts in crossbred (Bos taurus x Bos indicus) bulls
Yathish, H. M., Kumar, S., Dubey, P. P., Modi, R. P., Chaudhary, R., Siva Kumar, A., Ghosh, S. K., Sarkar, M., & Balasubramaniam, S. (2016) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2016.12.003 · Cited by 24
Iron–Sulfur Proteins and Iron–Sulfur Cluster Assembly in Organisms with Hydrogenosomes and Mitosomes
Tachezy, J., & Doležal, P. (2007) · Springer eBooks · doi:10.1007/978-3-540-38502-8_6 · Cited by 24
Arabidopsis cytosolic Nbp35 homodimer can assemble both [2Fe–2S] and [4Fe–4S] clusters in two distinct domains
Kohbushi, H., Nakai, Y., Kikuchi, S., Yabe‐Wada, T., Hori, H., & Nakai, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.138 · Cited by 24
The Archaeon Methanosarcina acetivorans Contains a Protein Disulfide Reductase with an Iron-Sulfur Cluster
Lessner, D. J., & Ferry, J. G. (2007) · Journal of Bacteriology · doi:10.1128/jb.00891-07 · Cited by 24
“Indeed, the genome of M. acetivorans does not encode complete homologs of known Fe-S cluster biosynthesis proteins (e.g., NifU, Nfu, and IscA) ( 33 , 40).”
Background
Methionine sulphoxide reductases protect iron–sulphur clusters from oxidative inactivation in yeast
Sideri, T. C., Willetts, S. A., & Avery, S. V. (2009) · Microbiology · doi:10.1099/mic.0.022665-0 · Cited by 24
“FeS clusters participate in electron transfer (featuring commonly in redox enzymes), substrate binding and activation, iron–sulphur storage and regulation of gene expression (Johnson et al., 2005).”
Fluorescent Probes for Tracking the Transfer of Iron–Sulfur Cluster and Other Metal Cofactors in Biosynthetic Reaction Pathways
Vranish, J. N., Russell, W. K., Yu, L. E., Cox, R. M., Russell, D. H., & Barondeau, D. P. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510998s · Cited by 23
Steps Toward Understanding Mitochondrial Fe/S Cluster Biogenesis
Melber, A., & Winge, D. R. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.09.004 · Cited by 25
Expanding the clinical and genetic spectrum of FDXR deficiency by functional validation of variants of uncertain significance
Stenton, S. L., Piekutowska‐Abramczuk, D., Kulterer, L., Kopajtich, R., Claeys, K. G., Ciara, E., Eisen, J., Płoski, R., Pronicka, E., Malczyk, K., et al. (2020) · Human Mutation · doi:10.1002/humu.24160 · Cited by 23
“S) clusters, integral to electron transport in mitochondrial respiration (Beilschmidt & Puccio, 2014; Ewen et al., 2011; Johnson et al., 2005; Jung et al., 1999; Stehling et al., 2014).”
Background
Methods to identify and characterize iron–sulfur oligopeptides in water
Valer, L., Rossetto, D., Scintilla, S., Hu, Y. J., Tomar, A., Nader, S., Betinol, I. O., & Mansy, S. S. (2022) · Canadian Journal of Chemistry · doi:10.1139/cjc-2021-0237 · Cited by 27
Exploiting Molecular Symmetry to Quantitatively Map the Excited-State Landscape of Iron–Sulfur Clusters
Skeel, B. A., & Suess, D. L. M. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c02412 · Cited by 23
SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea
Zafrilla, B., Martínez‐Espinosa, R. M., Esclapez, J., Pérez-Pomares, F., & Bonete, M.-J. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.03.001 · Cited by 23
Iron sulfur cluster biosynthesis. Human NFU mediates sulfide delivery to ISU in the final step of [2Fe–2S] cluster assembly
Liu, Y., & Cowan, J. A. (2007) · Chemical Communications · doi:10.1039/b704928e · Cited by 24
Identification of a Nfs1p-bound persulfide intermediate in Fe–S cluster synthesis by intact mitochondria
Pandey, A., Yoon, H., Lyver, E. R., Dancis, A., & Pain, D. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.07.103 · Cited by 23
“The substrate cysteine in the PLP adduct is converted to alanine and subsequently released, thereby regenerating PLP for a new catalytic cycle (Johnson et al., 2005; Mihara and Esaki, 2002; Selbach et al., 2010; Zheng et al., 1994).”
Background
Solvent‐ and Halide‐Induced (Inter)conversion between Iron(II)‐Disulfide and Iron(III)‐Thiolate Complexes
Wang, L., Reinhard, F. G. C., Philouze, C., Demeshko, S., de Visser, S. P., Meyer, F., Gennari, M., & Duboc, C. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201801377 · Cited by 23
Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity
Fox, N. G., Martelli, A., Nabhan, J. F., Janz, J. M., Borkowska, O., Bulawa, C., & Yue, W. W. (2018) · Biochimie · doi:10.1016/j.biochi.2018.07.012 · Cited by 22
Identification of IscU residues critical for de novo iron–sulfur cluster assembly
Tanaka, N., Yuda, E., Fujishiro, T., Hirabayashi, K., Wada, K., & Takahashi, Y. (2019) · Molecular Microbiology · doi:10.1111/mmi.14392 · Cited by 23
“Combination of IscU substitutions at Y3 and the IscS substitution at A349 modulated sulfur-transfer interaction C328 is a catalytic residue of IscS that eliminates the sulfur from L-cysteine substrate resulting in a C328-bound persulfide (R-S-SH).”
BackgroundInfluential
The Arabidopsis Mitochondrial Glutaredoxin GRXS15 Provides [2Fe-2S] Clusters for ISCA-Mediated [4Fe-4S] Cluster Maturation
Azam, T., Przybyla‐Toscano, J., Vignols, F., Couturier, J., Rouhier, N., & Johnson, M. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239237 · Cited by 23
“Therefore, cells use complex maturation systems to ensure the correct assembly, trafficking and insertion of Fe-S clusters [1,4,5].”
Background
Mycobacterium Sulfur Metabolism and Implications for Novel Drug Targets
Zeng, L., Shi, T., Zhao, Q., & Xie, J. (2012) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9410-x · Cited by 23
“Bacterial iron-sulfur clusters biosynthesis can be accomplished by three routes [36–40].”
Background
Structural Analysis of Arabidopsis CnfU Protein: An Iron–Sulfur Cluster Biosynthetic Scaffold in Chloroplasts
Yabe‐Wada, T., Yamashita, E., Kikuchi, A., Morimoto, K., Nakagawa, A., Tomitake Tsukihara, A., & Nakai, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.072 · Cited by 23
Insights into the role of nucleotide-dependent conformational change in nitrogenase catalysis: Structural characterization of the nitrogenase Fe protein Leu127 deletion variant with bound MgATP
Sen, S., Krishnakumar, A. M., McClead, J., Johnson, M. K., Seefeldt, L. C., Szilagyi, R. K., & Peters, J. W. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.02.016 · Cited by 23
Long-term suppression of Microcystis aeruginosa by tannic acid: Risks of microcystin pollution and proteomic mechanisms
Li, Y., Shi, K., Yin, Y. X., Zhang, Y., Xu, L., An, J., Peng, C., Wang, C., He, H., Yang, S., et al. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.137205 · Cited by 22

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
DOI: 10.1146/annurev.biochem.74.082803.133518
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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STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS

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