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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Background
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BackgroundInfluential
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Background
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Background
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Background
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Background
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BackgroundMethod
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Background
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Background
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“The regulation and biogenesis of Fe-S clusters have been extensively reviewed, and readers are encouraged to refer to these reviews [43,73,74].”
Background
FeoC from Klebsiella pneumoniae Contains a [4Fe-4S] Cluster
Hsueh, K.-L., Yu, L.-K., Chen, Y.-H., Cheng, Y.-H., Hsieh, Y., Ke, S., Hung, K., Chen, C., & Huang, T.-H. (2013) · Journal of Bacteriology · doi:10.1128/jb.00687-13 · Cited by 33
“Studies have documented several types of biological Fe-S clusters, including the simplest [1Fe] cluster in rubredoxin to the complex [8Fe-7S] cluster in nitrogenase (42, 49).”
Background
Insight into the protein and solvent contributions to the reduction potentials of [4Fe–4S]2+/+ clusters: crystal structures of the Allochromatium vinosum ferredoxin variants C57A and V13G and the homologous Escherichia coli ferredoxin
Saridakis, E., Giastas, P., Efthymiou, G., Thoma, V., Moulis, J., Kyritsis, P., & Mavridis, I. M. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0492-x · Cited by 33
Presence of P seudomonas aeruginosa influences biofilm formation and surface protein expression of S taphylococcus aureus
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Investigation of Iron-Sulfur Protein Maturation in Eukaryotes
Stehling, O., Smith, P., Biederbick, A., Balk, J., Lill, R., & Mühlenhoff, U. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-365-3_24 · Cited by 34
Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis
Fujishiro, T., Nakamura, R., Kunichika, K., & Takahashi, Y. (2022) · Biophysics and Physicobiology · doi:10.2142/biophysico.bppb-v19.0001 · Cited by 33
Protein expression profiles in patients carrying NFU1 mutations. Contribution to the pathophysiology of the disease
Ferrer-Cortés, X., Font, A., Bujan, N., Navarro‐Sastre, A., Matalonga, L., Arranz, J. A., Riudor, E., del Toro, M., García‐Cazorla, À., Campistol, J., et al. (2012) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-012-9565-z · Cited by 36
Biological iron-sulfur storage in a thioferrate-protein nanoparticle
Vaccaro, B. J., Clarkson, S. M., Holden, J. F., Lee, D.-W., Wu, C.-H., Poole, F. L., Cotelesage, J. J. H., Hackett, M. J., Mohebbi, S., Sun, J., et al. (2017) · Nature Communications · doi:10.1038/ncomms16110 · Cited by 33
Methyl ketone break-and-rebuild: a strategy for full α-heterofunctionalization of acetophenones
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Metagenomics-Guided Survey, Isolation, and Characterization of Uranium Resistant Microbiota from the Savannah River Site, USA
Jaswal, R., Pathak, A. K., Edwards, B., Lewis, R., III, Seaman, J. C., Stothard, P., Krivushin, K., Blom, J., Rupp, O., & Chauhan, A. (2019) · Genes · doi:10.3390/genes10050325 · Cited by 33
“It has been reported that the YgfZ proteins participate in assembly or repair of iron/sulfur clusters that perform a large number of conserved cellular processes such as catalysis, electron transport, gene regulation, DNA replication and repair, and central metabolism [80,81].”
Background
Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the mitochondrial iron-sulfur cluster assembly machinery
Nasta, V., Vela, S. D., Gourdoupis, S., Ciofi‐Baffoni, S., Svergun, D. I., & Banci, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-55313-5 · Cited by 32
The p53 Family: A Role in Lipid and Iron Metabolism
Laubach, K., Zhang, J., & Chen, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.715974 · Cited by 35
“Just before the turn of the century, the TP63 and TP73 genes were discovered due to their significant homology to TP53, particularly in the DNA-binding domain (Kaghad et al., 1997; Schmale and Bamberger, 1997; Trink et al., 1998; Borremans et al., 2001).”
Background
Rice folate enhancement through metabolic engineering has an impact on rice seed metabolism, but does not affect the expression of the endogenous folate biosynthesis genes
Blancquaert, D., Daele, J. V., Storozhenko, S., Stove, C. P., Lambert, W. E., & Straeten, D. V. D. (2013) · Plant Molecular Biology · doi:10.1007/s11103-013-0091-7 · Cited by 33
Formation of a Nitrogenase P‐cluster [Fe8S7] Core via Reductive Fusion of Two All‐Ferric [Fe4S4] Clusters
Ohki, Y., Tanifuji, K., Yamada, N., Cramer, R. E., & Tatsumi, K. (2012) · Chemistry - An Asian Journal · doi:10.1002/asia.201200568 · Cited by 33
Enterococcus faecalis SufU scaffold protein enhances SufS desulfurase activity by acquiring sulfur from its cysteine-153
Riboldi, G. P., de Oliveira, J. S., & Jeverson Frazzon, B. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.016 · Cited by 33
Genome Analysis of Chlamydomonas reinhardtii Reveals The Existence of Multiple, Compartmentalized Iron–Sulfur Protein Assembly Machineries of Different Evolutionary Origins
Godman, J., & Balk, J. (2008) · Genetics · doi:10.1534/genetics.107.086033 · Cited by 32
“NifU has a modular structure, with the modules often occurring as separate, single-domain proteins in other organisms (Mühlenhoff and Lill 2000; Johnson et al. 2005).”
BackgroundInfluential
Grip it and rip it: Structural mechanisms of DNA helicase substrate binding and unwinding
Bhattacharyya, B., & Keck, J. L. (2014) · Protein Science · doi:10.1002/pro.2533 · Cited by 35
“FeS clusters serve a variety of biological roles including electron transport, iron storage, protein stabilization, and oxidative stress sensors.(58) The presence of FeS clusters in nucleic acid processing enzymes was first discovered in the DNA glycosylase endonuclease III from E.”
Background
Dynamical magnetostructural properties of Anabaena ferredoxin
Schreiner, E., Nair, N. N., Pollet, R., Staemmler, V., & Marx, D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706740104 · Cited by 32
Anatomy of an iron-sulfur cluster scaffold protein: Understanding the determinants of [2Fe–2S] cluster stability on IscU
Adrover, M., Howes, B. D., Iannuzzi, C., Smulevich, G., & Pastore, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.023 · Cited by 32
A low band gap iron sulfide hybrid semiconductor with unique 2D [Fe16S20]8− layer and reduced thermal conductivity
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A [3Fe–3S] 3+ cluster with exclusively μ-sulfide donors
Lee, Y., Jeon, I., Abboud, K. A., García‐Serres, R., Shearer, J., & Murray, L. J. (2015) · Chemical Communications · doi:10.1039/c5cc07813j · Cited by 32
Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe–S cluster biogenesis regulation
Ciesielski, S. J., Schilke, B. A., Marszałek, J., & Craig, E. A. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-12-0815 · Cited by 32
“INTRODUCTION Iron–sulfur (Fe–S) clusters are essential cofactors of proteins engaged in fundamental cellular processes, such as oxidative phosphorylation, amino acid metabolism, ribosome assembly, and response to changing environmental conditions (Johnson et al., 2005).”
Background
Iron homeostasis in Mycobacterium tuberculosis is essential for persistence
Pandey, M., Talwar, S., Bose, S., & Pandey, A. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-35012-3 · Cited by 32
The Structure of the Dimeric State of IscU Harboring Two Adjacent [2Fe–2S] Clusters Provides Mechanistic Insights into Cluster Conversion to [4Fe–4S]
Kunichika, K., Nakamura, R., Fujishiro, T., & Takahashi, Y. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00112 · Cited by 32
Sustainable production of algae-bacteria granular consortia based biological hydrogen: New insights
Giri, D. D., Dwivedi, H., Alsukaibi, A. K. D., Pal, D. B., Otaibi, A. A., Areeshi, M. Y., Haque, S., & Gupta, V. K. (2022) · Bioresource Technology · doi:10.1016/j.biortech.2022.127036 · Cited by 32
Iron loading site on the Fe–S cluster assembly scaffold protein is distinct from the active site
Rodrigues, A. V., Kandegedara, A., Rotondo, J. A., Dancis, A., & Stemmler, T. L. (2015) · BioMetals · doi:10.1007/s10534-015-9846-8 · Cited by 31
“Iron-sulfur cluster containing proteins are utilized in all domains of life and found ubiquitously in nearly every cellular biochemical pathway (Johnson et al. 2005).”
Iron-Sulfur World in Aerobic and Hyperthermoacidophilic ArchaeaSulfolobus
Iwasaki, T. (2010) · Archaea · doi:10.1155/2010/842639 · Cited by 33
“In these tractable model organisms, the regulation of biological Fe-S cluster assembly is further complicated by the involvement of other accessory proteins required for the in vivo function [7, 8, 99, 101, 106, 107], and is not fully understood.”
Background
The A-type domain in Escherichia coli NfuA is required for regenerating the auxiliary [4Fe–4S] cluster in Escherichia coli lipoyl synthase
McCarthy, E. L., Rankin, A. N., Dill, Z., & Booker, S. J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006171 · Cited by 32
The chemical biology of hydrogen sulfide and related hydropersulfides: interactions with biologically relevant metals and metalloproteins
Fukuto, J. M., Vega, V. S., Works, C., & Lin, J. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.11.013 · Cited by 34
Molecular and regulatory mechanisms of oxidative stress adaptation in Streptococcus mutans
Yu, S., Ma, Q., Li, Y., & Zou, J. (2022) · Molecular Oral Microbiology · doi:10.1111/omi.12388 · Cited by 31
Understanding metal homeostasis in primary cultured neurons. Studies using single neuron subcellular and quantitative metallomics
Colvin, R. A., Lai, B. C. H., Holmes, W. R., & Lee, D. (2015) · Metallomics · doi:10.1039/c5mt00084j · Cited by 32
Iron–Sulfur Cluster Protein NITROGEN FIXATION S-LIKE1 and Its Interactor FRATAXIN Function in Plant Immunity
Fonseca, J. P., Lee, H., Boschiero, C., Griffiths, M., Lee, S., Zhao, P. X., York, L. M., & Mysore, K. S. (2020) · PLANT PHYSIOLOGY · doi:10.1104/pp.20.00950 · Cited by 31
“58 Several plant metabolic pathways and proteins require Fe-S clusters for proper functioning 59 (Johnson et al., 2005; Balk and Shaeddler, 2014).”
Background
Pathways of thymidine hypermodification
Lee, Y., Dai, N., Müller, S. I., Guan, C., Parker, M. J., Fraser, M. E., Walsh, S. E., Sridar, J., Mulholland, A. J., Nayak, K., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab781 · Cited by 31
Modulation of MagR magnetic properties via iron–sulfur cluster binding
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Weak Hydrogen Bonds Formed by Thiol Groups in N-Acetyl- l -Cysteine and Their Response to the Crystal Structure Distortion on Increasing Pressure
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Evaluation of Antibacterial and Antibiofilm Mechanisms by Usnic Acid Against Methicillin-Resistant Staphylococcus Aureus
Pompilio, A., Riviello, A., Crocetta, V., Giuseppe, F. D., Pomponio, S., Sulpizio, M., Ilio, C. D., Angelucci, S., Barone, L., Giulio, A. D., et al. (2016) · Future Microbiology · doi:10.2217/fmb-2016-0049 · Cited by 30
The H2O2-Resistant Fe–S Redox Switch MitoNEET Acts as a pH Sensor To Repair Stress-Damaged Fe–S Protein
Mons, C., Botzanowski, T., Nikolaev, A., Hellwig, P., Cianférani, S., Lescop, E., Bouton, C., & Golinelli‐Cohen, M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00777 · Cited by 33
A conserved motif liganding the [4Fe–4S] cluster in [4Fe–4S] fumarases prevents irreversible inactivation of the enzyme during hydrogen peroxide stress
Lu, Z., & Imlay, J. A. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101296 · Cited by 31
Sulfide and transition metals - A partnership for life
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Characterization and Crystallization of an IscU-type Scaffold Protein with Bound [2Fe 2S] Cluster from the Hyperthermophile, Aquifex aeolicus
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Transient iron coordination sites in proteins: Exploiting the dual nature of paramagnetic NMR
Piccioli, M., & Turano, P. (2014) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2014.05.007 · Cited by 30

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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