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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Yamanaka, Y., Zeppieri, L., Nicolet, Y., Marinoni, E. N., de Oliveira, J. S., Odaka, M., Dean, D. R., & Fontecilla-Camps, J. C. (2012) · Dalton Transactions · doi:10.1039/c2dt32101g · Cited by 18
ISCU interacts with NFU1, and ISCU[4Fe-4S] transfers its Fe-S cluster to NFU1 leading to the production of holo-NFU1
Cai, K., Frederick, R. O., & Markley, J. L. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2020.107491 · Cited by 19
“Fe-S clusters are ubiquitous protein factors that play important roles in a variety of important biological processes including electron transport, central metabolism, gene regulation, DNA repair and replication, and RNA modification (Rouault, 2012; Lill, 2009; Lill and Muhlenhoff, 2006; Johnson et al., 2005; Pain and…”
Background
During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1
Uzarska, M. A., Grochowina, I., Soldek, J., Jelen, M., Schilke, B. A., Marszałek, J., Craig, E. A., & Dutkiewicz, R. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101570 · Cited by 18
“(2022) 298(2) 101570 and Arg(318) of Nfs1, suggesting that Yah1 and Yfh1 use the same set of evolutionary conserved Nfs1 residues for their interaction with NIA–Isu1.”
BackgroundMethodInfluential
Iron–Sulfur Clusters toward Stresses: Implication for Understanding and Fighting Tuberculosis
Elchennawi, I., & de Choudens, S. O. (2022) · Inorganics · doi:10.3390/inorganics10100174 · Cited by 20
Transcriptome analysis reveals reasons for the low tolerance of Clostridium tyrobutyricum to furan derivatives
Suo, Y., Li, W., Wan, L., Luo, L., Liu, S., Qin, S., & Wang, J. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12281-7 · Cited by 18
The Interplay between Dysregulated Metabolism and Epigenetics in Cancer
Bassal, M. A. (2023) · Biomolecules · doi:10.3390/biom13060944 · Cited by 19
Dissecting the genetic architecture of root-related traits in a grafted wild Vitis berlandieri population for grapevine rootstock breeding
Blois, L., de Miguel, M., Bert, P., Ollat, N., Rubio, B., Voss‐Fels, K. P., Schmid, J., & Marguerit, E. (2023) · Theoretical and Applied Genetics · doi:10.1007/s00122-023-04472-1 · Cited by 18
“The chr9_18214759 marker was linked to the Vitvi09g00521 gene potentially involved in metal ion binding (Johnson et al. 2005), potentially accounting for the limestone tolerance of the V.”
Background
A tandem activity-based sensing and labeling strategy reveals antioxidant response element regulation of labile iron pools
Pezacki, A. T., Gonciarz, R. L., Okamura, T., Matier, C. D., Torrente, L., Cheng, K., Miller, S. G., Ralle, M., Ward, N. P., DeNicola, G. M., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2401579121 · Cited by 18
Biogenic pyrite and metastable iron sulfides: Emerging formation pathways and geological and societal relevance
Mansor, M., Duverger, A., Pasquier, V., Gorlas, A., Guyot, F., Berg, J. S., Marin‐Carbonne, J., Cosmidis, J., & Picard, A. (2025) · Geo-Bio Interfaces · doi:10.1180/gbi.2024.9 · Cited by 23
“Examples of Fe-S clusters are widespread in biogeochemistry, where they serve as active centres in essential proteins, including NADH dehydrogenase, coenzyme Q – cytochrome C reductase, hydrogenases and nitrogenase (Beinert, 2000; Johnson et al. , 2005; Huang et al. , 2024).”
Evidence that the Folate-Dependent Proteins YgfZ and MnmEG Have Opposing Effects on Growth and on Activity of the Iron-Sulfur Enzyme MiaB
Waller, J. C., Ellens, K. W., Hasnain, G., Alvarez, S., Rocca, J. R., & Hanson, A. D. (2011) · Journal of Bacteriology · doi:10.1128/jb.06226-11 · Cited by 18
“Fe-S clusters are highly versatile; the proteins that contain them play diverse roles in electron transfer, enzyme catalysis, and transcriptional regulation (17).”
Background
Role of the HSPA9/HSC20 chaperone pair in promoting directional human iron-sulfur cluster exchange involving monothiol glutaredoxin 5
Olive, J. A., & Cowan, J. A. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.04.007 · Cited by 18
IscR of Rhodobacter sphaeroides functions as repressor of genes for iron‐sulfur metabolism and represents a new type of iron‐sulfur‐binding protein
Remes, B., Eisenhardt, B. D., Srinivasan, V., & Klug, G. (2015) · MicrobiologyOpen · doi:10.1002/mbo3.279 · Cited by 18
“S clusters found in nature are the rhombic [2Fe–2S] and the cubane [4Fe–4S] clusters which contain either ferrous (Fe2+) or ferric (Fe3+) iron and sulfide (S2 ) (Drennan and Peters 2003; Johnson et al. 2005).”
Background
Enterococcus faecalis sufCDSUB complements Escherichia coli sufABCDSE
Riboldi, G. P., Larson, T. J., & Jeverson Frazzon, B. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02284.x · Cited by 18
“Iron–sulfur [Fe–S] clusters are inorganic prosthetic groups, widely distributed in nature, that play essential roles in diverse biological processes such as electron transfer, redox and nonredox catalysis, and gene regulation, and as sensors within all living organisms (Frazzon & Dean, 2003; Johnson et al., 2005).”
Background
Dissection of Hydrogen Bond Interaction Network around an Iron–Sulfur Cluster by Site-Specific Isotope Labeling of Hyperthermophilic Archaeal Rieske-Type Ferredoxin
Iwasaki, T., Fukazawa, R., Miyajima-Nakano, Y., Baldansuren, A., Matsushita, S., Lin, M. T., Gennis, R. B., Hasegawa, K., Kumasaka, T., & Dikanov, S. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja308049u · Cited by 19
Density functional theory calculations of redox properties of iron–sulphur protein analogues
Niu, S., & Ichiye, T. (2011) · Molecular Simulation · doi:10.1080/08927022.2011.582111 · Cited by 19
“For instance, the Fe–S cluster assembly mechanism of certain Fe–S proteins is thought to entail assembling a [4Fe–4S] cluster on a scaffold protein and then transferring half of the cluster at a time to a target protein [ 115 ].”
Background
The Molecular Determinants of the Increased Reduction Potential of the Rubredoxin Domain of Rubrerythrin Relative to Rubredoxin
Luo, Y., Ergenekan, C. E., Fischer, J. T., Tan, M., & Ichiye, T. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.11.006 · Cited by 18
Electron transfer between [4Fe–4S] clusters
Voityuk, A. A. (2010) · Chemical Physics Letters · doi:10.1016/j.cplett.2010.06.057 · Cited by 18
Stabilities of cubane type [Fe4S4(SR)4]2− clusters in partially aqueous media
Lo, W., Scott, T. A., Zhang, P., Ling, C., & Holm, R. H. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2010.12.009 · Cited by 18
Hydrogenases and Hydrogen Metabolism in Photosynthetic Prokaryotes
Schwarz, C., Poss, Z. C., Hoffmann, D., & Appel, J. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-1528-3_18 · Cited by 18
Chapter 42 Techniques to Isolate O2-Sensitive Proteins
Yan, A., & Kiley, P. J. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)63042-1 · Cited by 18
“coli ( Johnson et al., 2005; Kiley and Beinert, 2003).”
Differentiation of sow and mouse ovarian granulosa cells exposed to zearalenone in vitro using RNA-seq gene expression
Zhang, G., Song, J., Zhou, Y. J., Zhang, R., Cheng, S., Sun, X., Qin, G., Shen, W., & Li, L. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.05.003 · Cited by 18
Identification of Genes Involved in Fe–S Cluster Biosynthesis of Nitrogenase in Paenibacillus polymyxa WLY78
Li, Q., Li, Y., Li, X., & Chen, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073771 · Cited by 17
“In addition to the Nif system that is specifically responsible for the synthesis of the Fe–S clusters of nitrogenase, Isc and Suf are required for a broad range of cell functions [5].”
Background
Mining anion–aromatic interactions in the Protein Data Bank
Kuźniak, E., Glanowski, M., Kurczab, R., Bojarski, A. J., & Podgajny, R. (2022) · Chemical Science · doi:10.1039/d2sc00763k · Cited by 17
The Intriguing mitoNEET: Functional and Spectroscopic Properties of a Unique [2Fe-2S] Cluster Coordination Geometry
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Towards magnetism in pigeon MagR: Iron- and iron-sulfur binding work indispensably and synergistically
Zhou, Y., 安徽大学物质科学与信息技术学院, 安. 合. 2., Tong, T., Wei, M., Zhang, P., Fei, F., Zhou, X., Guo, Z., Zhang, J., Xu, H., et al. (2022) · 动物学研究 · doi:10.24272/j.issn.2095-8137.2022.423 · Cited by 18
“Iron-sulfur proteins, among the most ancient metalloproteins on Earth, serve as electron carriers in all kingdoms of life due to the redox properties of iron-sulfur clusters (Johnson et al., 2005; Kiley & Beinert, 2003; Lill, 2009).”
Background
Review: Advances in the Accuracy and Traceability of Metalloprotein Measurements Using Isotope Dilution Inductively Coupled Plasma Mass Spectrometry
Coverdale, J. P. C., Harrington, C. F., & Solovyev, N. D. (2023) · Critical Reviews in Analytical Chemistry · doi:10.1080/10408347.2022.2162811 · Cited by 17
“[37,38] A strict redox balance and highly regulated homeostasis of iron in the body is mandatory.”
Facile and dynamic cleavage of every iron–sulfide bond in cuboidal iron–sulfur clusters
Thompson, N. B., Namkoong, G., Skeel, B. A., & Suess, D. L. M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210528120 · Cited by 17
Recent Advances, Challenges, and Metabolic Engineering Strategies in L-Cysteine Biosynthesis
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Human ferredoxin-2 displays a unique conformational change
Qi, W., Li, J., & Cowan, J. A. (2012) · Dalton Transactions · doi:10.1039/c2dt32018e · Cited by 17
X-ray structures of Nfs2, the plastidial cysteine desulfurase fromArabidopsis thaliana
Roret, T., Pégeot, H., Couturier, J., Mulliert, G., Rouhier, N., & Claude Didierjean, B. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14017026 · Cited by 18
“S] clusters (Mihara et al., 2002; Mühlenhoff et al., 2004; Johnson et al., 2005).”
Ecologically adaptable Populus simonii is specific for recalcitrance‐reduced lignocellulose and largely enhanced enzymatic saccharification among woody plants
Lv, Z., Liu, F., Zhang, Y., Tu, Y., Chen, P., & Peng, L. (2020) · GCB Bioenergy · doi:10.1111/gcbb.12764 · Cited by 17
“…binding, which was associated with iron–sulfur storage, electron transfer, substrate activation, regulation of enzyme activity and gene expression (Johnson et al., 2005), was identified from the co-upregulated DEGs (Figure 6d), but 12 specific GO terms were enriched for the co-downregulated…”
Background
Functional implications of the interaction between HscB and IscU in the biosynthesis of FeS clusters
Iametti, S., Barbiroli, A. G., & Bonomi, F. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1285-z · Cited by 17
Global Identification of Genes Affecting Iron-Sulfur Cluster Biogenesis and Iron Homeostasis
Hidese, R., Mihara, H., Kurihara, T., & Esaki, N. (2014) · Journal of Bacteriology · doi:10.1128/jb.01160-13 · Cited by 17
“The most abundant types of Fe-S clusters are rhombic [2Fe2S] and cubane [4Fe-4S] (2, 4), in which the iron atoms are generally bound to the sulfur atoms in the cysteine residues of the peptide backbone and to inorganic sulfurs in the prosthetic group.”
Background
The reduced [2Fe-2S] clusters in adrenodoxin and Arthrospira platensis ferredoxin share spin density with protein nitrogens, probed using 2D ESEEM
Dikanov, S. A., Samoilova, R. I., Kappl, R., Crofts, A. R., & Hüttermann, J. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b904597j · Cited by 17

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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