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

The DOI matches its Crossref record; 209 of the 209 references it cites were found in a registry or an index.

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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10.1074/jbc.275.12.8283 · DOI
10.1074/jbc.M104067200 · DOI

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Background
Formation of [4Fe-4S] Clusters in the Mitochondrial Iron–Sulfur Cluster Assembly Machinery
Brancaccio, D., Gallo, A., Mikołajczyk, M., Zovo, K., Palumaa, P., Novellino, E., Piccioli, M., Ciofi‐Baffoni, S., & Banci, L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja507822j · Cited by 130
A review of the concepts, recent advances and niche applications of the (photo) Fenton process, beyond water/wastewater treatment: Surface functionalization, biomass treatment, combatting cancer and other medical uses
Giannakis, S. (2019) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2019.02.025 · Cited by 135
The Essential WD40 Protein Cia1 Is Involved in a Late Step of Cytosolic and Nuclear Iron-Sulfur Protein Assembly
Balk, J., Netz, D. J. A., Tepper, K., Pierik, A. J., & Lill, R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10833-10841.2005 · Cited by 129
“Many proteins have now been shown to be required for assembly and insertion of the deceivingly simple [2Fe-2S] and cubane [4Fe-4S] clusters into bacterial apoproteins (13).”
Background
Crystal structure of human mitoNEET reveals distinct groups of iron–sulfur proteins
Lin, J., Zhou, T., Ye, K., & Wang, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702426104 · Cited by 135
Deletion of iscR stimulates recombinant clostridial Fe–Fe hydrogenase activity and H2-accumulation in Escherichia coli BL21(DE3)
Akhtar, M. K., & Jones, P. R. (2008) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-008-1377-6 · Cited by 130
Small-Molecule Fluorescent Probes for Binding- and Activity-Based Sensing of Redox-Active Biological Metals
Grover, K., Koblova, A., Pezacki, A. T., Chang, C. J., & New, E. J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00819 · Cited by 129
Sequence-Specific Binding to a Subset of IscR-Regulated Promoters Does Not Require IscR Fe–S Cluster Ligation
Nesbit, A. D., Giel, J. L., Rose, J. C., & Kiley, P. J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.055 · Cited by 125
The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
Uzarska, M. A., Dutkiewicz, R., Freibert, S., Lill, R., & Mühlenhoff, U. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-09-0644 · Cited by 133
“In the mitochondrial ISC assembly system the de novo synthesis of Fe/S clusters is accomplished on the scaffold protein Isu1 (related to bacterial IscU; Johnson et al., 2005; Lill and Muhlenhoff, 2006, 2008; Fontecave and Ollagnier-de-Choudens, 2008; Ye and Rouault, 2010).”
BackgroundMethod
The Interplay between Intracellular Iron Homeostasis and Neuroinflammation in Neurodegenerative Diseases
Lee, J., & Hyun, D. (2023) · Antioxidants · doi:10.3390/antiox12040918 · Cited by 142
“Iron is an essential cofactor for iron-dependent enzymes that require iron–sulfur clusters for proper function, which transfer an electron to targets [24].”
Background
Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle
Sendamarai, A. K., Ohgami, R. S., Fleming, M. D., & Lawrence, C. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801318105 · Cited by 134
Stabilization of Fully Reduced Iron−Sulfur Clusters by Carbene Ligation: The [FenSn]0 Oxidation Levels (n = 4, 8)
Deng, L., & Holm, R. H. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802111w · Cited by 127
Metal Binding Proteins
Permyakov, E. A. (2021) · Encyclopedia · doi:10.3390/encyclopedia1010024 · Cited by 132
Iron–sulfur cluster synthesis, iron homeostasis and oxidative stress in Friedreich ataxia
Vaubel, R. A., & Isaya, G. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.08.003 · Cited by 123
“DEFICIENT ISC SYNTHESIS AND THE PATHOPHYSIOLOGY OF FRDA ISC are essential and highly adaptable enzyme co-factors that can participate in a wide range of cellular reactions and processes [reviewed in (Johnson et al., 2005)].”
Background
Transcriptome Analysis of Escherichia coli O157:H7 Exposed to Lysates of Lettuce Leaves
Kyle, J. L., Parker, C. T., Goudeau, D., & Brandl, M. T. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.02461-09 · Cited by 119
“The IscR-regulated gene cluster iscRSUA-hscBAfdx-iscX, which is associated with Fe-S cluster assembly and repair (34), was highly upregulated at 30 min postexposure to lettuce lysates (including upregulation of iscR itself as soon as 15 min postinoculation).”
Background
Protein networks in the maturation of human iron–sulfur proteins
Ciofi‐Baffoni, S., Nasta, V., & Banci, L. (2017) · Metallomics · doi:10.1039/c7mt00269f · Cited by 119
Cysteine Is Not the Sulfur Source for Iron-Sulfur Cluster and Methionine Biosynthesis in the Methanogenic Archaeon Methanococcus maripaludis
Liu, Y., Sieprawska‐Lupa, M., Whitman, W. B., & White, R. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.152447 · Cited by 123
Biogenesis of the cytochrome bc1 complex and role of assembly factors
Smith, P. M., Fox, J. L., & Winge, D. R. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.11.009 · Cited by 128
Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity
Rajagopalan, S., Teter, S. J., Zwart, P. H., Brennan, R. G., Phillips, K. J., & Kiley, P. J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2568 · Cited by 118
“They play key structural, catalytic, or electron transfer roles in genome maintenance, transcription, translation, and metabolism 1 .”
Controlled Expression and Functional Analysis of Iron-Sulfur Cluster Biosynthetic Components within Azotobacter vinelandii
Johnson, D. C., Unciuleac, M.-C., & Dean, D. R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00596-06 · Cited by 118
“IscU proteins are also distinguished from the SufU class in that they have a conserved His105 residue that is replaced by lysine in SufU proteins.”
Background
H2 Conversion in the Presence of O2 as Performed by the Membrane‐Bound [NiFe]‐Hydrogenase of Ralstonia eutropha
Lenz, O., Ludwig, M., Schubert, T., Bürstel, I., Ganskow, S., Goris, T., Schwarze, A., & Friedrich, B. (2010) · ChemPhysChem · doi:10.1002/cphc.200901002 · Cited by 116
Mitochondrial iron metabolism and neurodegenerative diseases
Cheng, R., Dhorajia, V. V., Kim, J., & Kim, Y. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.11.003 · Cited by 121
Analysis of the Heteromeric CsdA-CsdE Cysteine Desulfurase, Assisting Fe-S Cluster Biogenesis in Escherichia coli
Loiseau, L., de Choudens, S. O., Lascoux, D., Forest, É., Fontecave, M., & Barras, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504067200 · Cited by 116
The SufBCD Fe−S Scaffold Complex Interacts with SufA for Fe−S Cluster Transfer
Chahal, H. K., Dai, Y., Saini, A. K., Ayala-Castro, C. N., & Outten, F. W. (2009) · Biochemistry · doi:10.1021/bi901518y · Cited by 116
“coli (7-11), but is the sole cluster assembly system in other prokaryotes and in the chloroplast of some photosynthetic eukaryotes (11-13).”
Background
Mechanisms of iron–sulfur cluster assembly: the SUF machinery
Fontecave, M., de Choudens, S. O., Py, B., & Barras, F. (2005) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-005-0025-1 · Cited by 117
Methanogens: a window into ancient sulfur metabolism
Liu, Y., Beer, L. L., & Whitman, W. B. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.02.002 · Cited by 113
New method for quantification of gasotransmitter hydrogen sulfide in biological matrices by LC-MS/MS
Tan, B., Jin, S., Sun, J., Gu, Z., Sun, X., Zhu, Y., Huo, K., Cao, Z., Yang, P., Liu, X., et al. (2017) · Scientific Reports · doi:10.1038/srep46278 · Cited by 113
Transcriptional Profiling of Nitrogen Fixation in Azotobacter vinelandii
Hamilton, T. L., Ludwig, M., Dixon, R. A., Boyd, E. S., Santos, P. C. D., Setúbal, J. C., Bryant, D. A., Dean, D. R., & Peters, J. W. (2011) · Journal of Bacteriology · doi:10.1128/jb.05099-11 · Cited by 111
“The more general components of the machinery responsible for maturation of “housekeeping” [Fe-S] proteins have been designated ISC components and include iscR, iscU, iscS, iscA, hscB hscA, fdx, and iscX (Avin40340 to Avin40410) (38).”
Background
Global Transcriptional Analysis of Dehydrated Salmonella enterica Serovar Typhimurium
Gruzdev, N., McClelland, M., Porwollik, S., Ofaim, S., Pinto, R., & Sela, S. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.01822-12 · Cited by 117
“FNR oxygen sensing is mediated by oxygen-induced conversion of the DNAbinding dimeric [4Fe-4S](2) cluster to a monomeric [2Fe-2S](2) form (38).”
Background
Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
Hausmann, A., Samans, B., Lill, R., & Mühlenhoff, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705570200 · Cited by 111
A Proposed Role for the Azotobacter vinelandii NfuA Protein as an Intermediate Iron-Sulfur Cluster Carrier
Bandyopadhyay, S., Naik, S., O’Carroll, I. P., Huynh, B.-H., Dean, D. R., Johnson, M. K., & Santos, P. C. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709161200 · Cited by 111
Transcription Factor NsrR from Bacillus subtilis Senses Nitric Oxide with a 4Fe−4S Cluster
Yukl, E. T., Elbaz, M. A., NAKANO, M. M., & Moënne‐Loccoz, P. (2008) · Biochemistry · doi:10.1021/bi801342x · Cited by 110
Monothiol glutaredoxins and A-type proteins: partners in Fe–S cluster trafficking
Mapolelo, D. T., Zhang, B., Randeniya, S., Albetel, A., Li, H., Couturier, J., Outten, C. E., Rouhier, N., & Johnson, M. K. (2012) · Dalton Transactions · doi:10.1039/c2dt32263c · Cited by 110
Oxidant-Responsive Induction of the suf Operon, Encoding a Fe-S Assembly System, through Fur and IscR in Escherichia coli
Lee, K.-C., Yeo, W., & Roe, J. (2008) · Journal of Bacteriology · doi:10.1128/jb.01161-08 · Cited by 108
A novel ICT-based two photon and NIR fluorescent probe for labile Fe2+ detection and cell imaging in living cells
Yang, X., Wang, Y., Liu, R., Zhang, Y., Tang, J., Yang, E., Zhang, D., Zhao, Y., & Ye, Y. (2019) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2019.02.123 · Cited by 108
Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS
Hoewyk, D. V., Abdel‐Ghany, S. E., Cohu, C. M., Herbert, S. K., Kugrens, P., Pilon, M., & Pilon‐Smits, E. A. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700774104 · Cited by 108
Measurement of H2S In Vivo and In Vitro by the Monobromobimane Method
Shen, X., Kolluru, G. K., Yuan, S. S., & Kevil, C. G. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2014.11.039 · Cited by 108
“Acid-labile sulfide consists of sulfur present in the iron-sulfur clusters contained in iron-sulfur proteins (Johnson et al., 2005).”
Background
Activity-based sensing fluorescent probes for iron in biological systems
Aron, A. T., Reeves, A. G., & Chang, C. J. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.12.010 · Cited by 111
Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors
Hidese, R., Mihara, H., & Esaki, N. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3336-x · Cited by 111
“Fe–S clusters, which are thought to be among the earliest catalysts in the evolution of biomolecules, serve as electron carriers in redox reactions, regulatory sensors, stabilizers of protein structure, and chemical catalysts (Beinert 2000; Johnson et al. 2005; Py and Barras 2010).”
BackgroundInfluential
SufU Is an Essential Iron-Sulfur Cluster Scaffold Protein in Bacillus subtilis
Albrecht, A. G., Netz, D. J. A., Miethke, M., Pierik, A. J., Burghaus, O., Peuckert, F., Lill, R., & Marahiel, M. A. (2010) · Journal of Bacteriology · doi:10.1128/jb.01536-09 · Cited by 110
“The SufU (YurV) protein sequence shows significant differences from alignments of IscU-type scaffold protein sequences (24).”
BackgroundInfluential
Cytosolic Iron-Sulfur Cluster Assembly (CIA) System: Factors, Mechanism, and Relevance to Cellular Iron Regulation
Sharma, A. K., Pallesen, L. J., Spang, R. J., & Walden, W. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.122218 · Cited by 113
Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis
Stehling, O., Netz, D. J. A., Niggemeyer, B., Rösser, R., Eisenstein, R. S., Puccio, H. M., Pierik, A. J., & Lill, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00545-08 · Cited by 107
“Proteins carrying iron-sulfur (Fe/S) clusters as inorganic cofactors are involved in fundamental cellular processes such as respiration, enzyme catalysis, and regulation of gene expression (6, 28), accounting for their presence in all kingdoms of life.”
Background
NifB-dependent in vitro synthesis of the iron–molybdenum cofactor of nitrogenase
Curatti, L., Ludden, P. W., & Rubio, L. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601115103 · Cited by 109

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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