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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A theoretical investigation on geometry and electronic structure of small FemSn nanoclusters (1⩽m,n⩽4)
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Differential expression of cysteine desulfurases in soybean
Heis, M. D., Ditmer, E. M., de Oliveira, L. A., Frazzon, A. P. G., Margis, R., & Jeverson Frazzon, B. (2011) · BMC Plant Biology · doi:10.1186/1471-2229-11-166 · Cited by 13
“Besides, [FeS] clusters are involved in sensing environmental stimuli and regulation of protein expression [1-3].”
Background
The Zn- and Cd-Clusters of Recombinant Mammalian MT1 and MT4 Metallothionein Domains Include Sulfide Ligands
Tío, L., Villarreal, L., Atrian, S., & Capdevila, M. (2006) · Experimental Biology and Medicine · doi:10.1177/153537020623100911 · Cited by 13
Differential expression of iron–sulfur cluster biosynthesis genes during peach fruit development and ripening, and their response to iron compound spraying
Song, Z., Ma, R., Zhang, B., Guo, S., Yu, M., & Korir, N. K. (2016) · Scientia Horticulturae · doi:10.1016/j.scienta.2016.05.024 · Cited by 13
NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis
Cai, K., & Markley, J. L. (2018) · Molecules · doi:10.3390/molecules23092213 · Cited by 15
“The ISC machinery, encoded by the iscRSUA operon, contains the following components: IscR (transcription factor that regulates the expression of the iscRSUA operon in response to the iron-sulfur cluster content of the cell), IscS (cysteine desulfurase), IscU (scaffold protein for de novo Fe-S cluster assembly), IscA (…”
BackgroundInfluential
SufR, a [4Fe-4S] Cluster-Containing Transcription Factor, Represses the sufRBDCSU Operon in Streptomyces avermitilis Iron-Sulfur Cluster Assembly
Cheng, Y., Lyu, M., Yang, R., Wen, Y., Song, Y., Li, J., & Chen, Z. (2020) · Applied and Environmental Microbiology · doi:10.1128/aem.01523-20 · Cited by 13
“the Nif (nitrogen fixation) system (2, 4).”
Characterization of Fe-S Clusters in Proteins by Mӧssbauer Spectroscopy
Ueda, C., Langton, M., & Pandelia, M. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1605-5_15 · Cited by 13
Methanosarcina acetivorans contains a functional ISC system for iron-sulfur cluster biogenesis
Deere, T. M., Prakash, D., Lessner, F. H., Duin, E. C., & Lessner, D. J. (2020) · BMC Microbiology · doi:10.1186/s12866-020-02014-z · Cited by 12
Streptococcus mutans Lacking sufCDSUB Is Viable, but Displays Major Defects in Growth, Stress Tolerance Responses and Biofilm Formation
Ellepola, K., Huang, X., Riley, R. P., Bitoun, J. P., & Wen, Z. T. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.671533 · Cited by 12
Enhanced fermentative biohydrogen production from milk processing wastewater by magnetic spinel ferrites nanoparticles
Lakroun, S. E., Boutemak, K., Haddad, A., Bouchareb, E. M., & Bouchareb, R. (2023) · Energy Sources Part A Recovery Utilization and Environmental Effects · doi:10.1080/15567036.2023.2193562 · Cited by 12
“…revealed that iron-sulfur clusters Fe-S are sensitive and exhibit a binding ability to cobalt ions at an excessive amount (Ranquet et al. 2007) knowing that Fe-S clusters play a critical role in electron transfer within ferredoxin proteins and b-subunit of [Ni-Fe] hydrogenase (Johnson et al. 2005).”
Background
The Bioinorganic Chemistry of the First Row d-Block Metal Ions—An Introduction
Marques, H. M. (2025) · Inorganics · doi:10.3390/inorganics13050137 · Cited by 14
Secondary Metabolism for Isoprenoid-based Biofuels
Kang, A., & Lee, T. S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-444-63475-7.00002-9 · Cited by 13
1.2 Å resolution crystal structure of the periplasmic aminotransferase PvdN fromPseudomonas aeruginosa
Drake, E. J., & Gulick, A. M. (2016) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x16006257 · Cited by 12
“S) cluster biosynthetic systems (Johnson et al., 2005).”
Defining the domains of Cia2 required for its essential function in vivo and in vitro
Vo, A., Fleischman, N. M., Marquez, M. D., Camire, E. J., Esonwune, S., Grossman, J. D., Gay, K. A., Cosman, J. A., & Perlstein, D. L. (2017) · Metallomics · doi:10.1039/c7mt00181a · Cited by 11
Transcript profiling of the immunological interactions between Actinobacillus pleuropneumoniae serotype 7 and the host by dual RNA-seq
Li, P., Xu, Z., Sun, X., Yin, Y., Fan, Y., Zhao, J., Xiyu, M., Huang, J., Yang, F., & Zhu, L. (2017) · BMC Microbiology · doi:10.1186/s12866-017-1105-4 · Cited by 12
Interaction of ferritin iron responsive element (IRE) mRNA with translation initiation factor eIF4F
Khan, M. A., Malik, A., Domashevskiy, A., San, A., & Khan, J. M. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.118776 · Cited by 13
Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa
Vallée, Y., & Youssef‐Saliba, S. (2021) · Synthesis · doi:10.1055/a-1472-7914 · Cited by 12
Histidine Ligated Iron‐Sulfur Peptides
Valer, L., Rossetto, D., Parkkila, T., Sebastianelli, L., Guella, G., Hendricks, A. L., Cowan, J. A., Sang, L., & Mansy, S. S. (2022) · ChemBioChem · doi:10.1002/cbic.202200202 · Cited by 12
Maturation strategy influences expression levels and cofactor occupancy in Fe–S proteins
Jansing, M., Mielenbrink, S., Rosenbach, H., Metzger, S. U., & Span, I. (2022) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-022-01972-1 · Cited by 12
“BL21(DE3) have been routinely used to express Fe–S proteins, as they harbor the ISC and SUF iron–sulfur cluster assembly machineries [59, 60].”
Method
The influence of oxygen and electronegativity on iron mineral chemistry throughout Earth’s history
Moore, E. K., Ostroverkhova, A., Hummer, D. R., Morrison, S. M., Peralta, Y., & Spielman, S. J. (2023) · Precambrian Research · doi:10.1016/j.precamres.2022.106960 · Cited by 12
Matrix-assisted refolding and redox properties of WhiB3/Rv3416 of Mycobacterium tuberculosis H37Rv
Alam†, M. S., & Agrawal, P. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.04.010 · Cited by 12
Novel iminopyridine derivatives: ligands for preparation of Fe( ii ) and Cu( ii ) dinuclear complexes
Martínez‐Ferraté, O., Lopez-Valbuena, J. M., Belmonte, M. M., White, A. J. P., Benet‐Buchholz, J., Britovsek, G. J. P., Claver, C., & van Leeuwen, P. W. N. M. (2016) · Dalton Transactions · doi:10.1039/c5dt04358a · Cited by 12
Methods for Studying Iron Regulatory Protein 1: An Important Protein in Human Iron Metabolism
Holmes‐Hampton, G. P., Ghosh, M. C., & Rouault, T. A. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.09.006 · Cited by 13
The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis
Pardoux, R., Fiévet, A., Carreira, C., Brochier‐Armanet, C., Valette, O., Dermoun, Z., Py, B., Dolla, A. R., Pauleta, S. R., & Aubert, C. (2019) · Scientific Reports · doi:10.1038/s41598-018-37021-8 · Cited by 12
Generation of H2S from Thiol-Dependent NO Reactivity of Model [4Fe-4S] Cluster and Roussin’s Black Anion
Oakley, K., Zhao, Z., Lehane, R. L., Ma, J., & Kim, E. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c01328 · Cited by 12
Genome Wide Re-Annotation of Caldicellulosiruptor saccharolyticus with New Insights into Genes Involved in Biomass Degradation and Hydrogen Production
Chowdhary, N., Selvaraj, A., KrishnaKumaar, L., & Kumar, G. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133183 · Cited by 12
Mitochondrial iron metabolism in plants: frataxin comes into play
Murgia, I., Tarantino, D., & Soave, C. (2009) · Plant and Soil · doi:10.1007/s11104-009-0038-6 · Cited by 12
“…bacterial ISC machinery (Iron Sulfur Cluster), formed by the gene cluster IscS, IscU, an alternative scaffold protein IscA, two heat shock proteins (HscA and HscB), ferredoxin Fdx and the Fe-S cluster assembly regulatory protein IscR (Balk and Lobreaux 2005; Johnson et al. 2005; Briat et al. 2007).”
Background
Cubane-Type Fe4S4 Clusters with Chiral Thiolate Ligation: Formation by Ligand Substitution, Detection of Intermediates by 1H NMR, and Solid State Structures Including Spontaneous Resolution Upon Crystallization
Lo, W., Huang, S., Zheng, S., & Holm, R. H. (2011) · Inorganic Chemistry · doi:10.1021/ic2016269 · Cited by 12
Mutational analysis of YgfZ, a folate-dependent protein implicated in iron/sulphur cluster metabolism
Hasnain, G., Waller, J. C., Alvarez, S., Ravilious, G. E., Jez, J. M., & Hanson, A. D. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02448.x · Cited by 12
“Although Fe/S clusters are structurally simple, their assembly depends on complex machinery, the components of which are still not fully known (Johnson et al., 2005; Fontecave & Ollagnier de Choudens, 2008).”
Background
The Origin of Life: Look Up and Look Down
Peters, J. W., & Williams, L. D. (2012) · Astrobiology · doi:10.1089/ast.2012.0818 · Cited by 14
“Iron-sulfur proteins are ubiquitous enzymes in life (Holm et al., 1996; Beinert et al., 1997; Johnson, 1998; Beinert, 2000; Noodleman et al., 2002; Johnson et al., 2005) and are integral to energy metabolism.”
Selenate reductase activity inEscherichia colirequires Isc iron-sulfur cluster biosynthesis genes
Yee, N., Choi, J. K., Porter, A. W., Carey, S., Rauschenbach, I., & Harel, A. (2014) · FEMS Microbiology Letters · doi:10.1111/1574-6968.12623 · Cited by 12
“The DnaK molecular chaperone is a close homolog of HscA (Johnson et al., 2005; AyalaCastro et al., 2008; Py & Barras, 2010; Roche et al., 2013) and is known to interact with the selenate reductase maturation protein DmsD (Oresnik et al., 2001; Guymer et al., 2009; Li et al., 2010).”
BackgroundInfluential
Phosphorothioated DNA Is Shielded from Oxidative Damage
Pu, T., Liang, J., Mei, Z., Yang, Y., Wang, J., Zhang, W., Liang, W., Zhou, X., Deng, Z., & Wang, Z. (2019) · Applied and Environmental Microbiology · doi:10.1128/aem.00104-19 · Cited by 12
“In biological systems iron-sulfur (Fe-S) metalloproteins can have their Fe-S atoms arranged in a number of different ways (22).”
BackgroundInfluential
Fighting ischemia-reperfusion injury: Focusing on mitochondria-derived ferroptosis
Tian, L., Liu, Q., Guo, H. W., Zang, H., & Li, Y. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101974 · Cited by 15
S-adenosyl-L-methionine is the unexpected methyl donor for the methylation of mercury by the membrane-associated HgcAB complex
Zheng, K., Rush, K. W., Date, S. S., Johs, A., Parks, J. M., Fleischhacker, A. S., Abernathy, M. J., Sarangi, R., & Ragsdale, S. W. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2408086121 · Cited by 11
Isd11p Protein Activates the Mitochondrial Cysteine Desulfurase Nfs1p Protein
Pandey, A., Yoon, H., Lyver, E. R., Dancis, A., & Pain, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.288522 · Cited by 11
Retracted

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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