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
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Fe-S clusters are ubiquitous, inorganic co-factors that contribute to a wide range of cellular pathways from genome integrity and gene regulation to energy production and immune responses, and are required for numerous biological functions, particularly enzymatic activity (Beinert, 2000; Johnson et al., 2005; Lee et al., 2009; Fuss et al., 2015).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Johnson et al., 2005
In the citing paper
“iron can act alone or in iron–sulfur clusters as a prosthetic moiety for members of the oxidoreductase, nitrogenase, hydrogenase, dehydrogenase, and hydratase enzyme families [7–12].”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [11]
Citations
Cites
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
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891
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
Cited by
Sorted by citations
Items 901–1,000 of 1,000
“Iron priming” guides folding of denatured aporubredoxins
Bonomi, F., Iametti, S., Ferranti, P., Kurtz, D. M. J., Morleo, A., & Ragg, E. M. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0385-4 · Cited by 11
Vecchio, M. D., Pogni, R., Baratto, M. C., Nobbs, A. H., Rappuoli, R., Pizza, M., & Balducci, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057547 · Cited by 11
Photo-Enzymatic Green Synthesis: The Potential of Combining Photo-Catalysis and Enzymes
Patil, P. D., Nadar, S. S., & Marghade, D. T. (2021) · Advances in Science, Technology & Innovation/Advances in science, technology & innovation · doi:10.1007/978-3-030-67884-5_9 · Cited by 12
Lin, C.-W., Oney-Hawthorne, S. D., Kuo, S.-T. A., Barondeau, D. P., & Russell, D. H. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00429 · Cited by 12
Pandey, A. K., Pain, J., Brindha, J., Dancis, A., & Pain, D. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.02.006 · Cited by 11
Decreased Transport Restores Growth of a Salmonella enterica apbC Mutant on Tricarballylate
Boyd, J. M., Teoh, W. P., & Downs, D. M. (2011) · Journal of Bacteriology · doi:10.1128/jb.05988-11 · Cited by 11
“With the exception of ErpA, NifU, and ApbC, genetic evidence to suggest preferential cellular targets for these [Fe-S] cluster scaffolding/trafficking proteins remains to be reported (26, 35).”
BackgroundSulfide ions as modulators of metal–thiolate cluster size in a plant metallothionein
Huber, T., & Freisinger, E. (2013) · Dalton Transactions · doi:10.1039/c3dt32438a · Cited by 11
Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals
Guo, Y., Brecht, E., Aznavour, K., Nix, J. C., Xiao, Y., Wang, H., George, S. J., Bau, R., Keable, S. M., Peters, J. W., et al. (2012) · Hyperfine Interactions · doi:10.1007/s10751-012-0643-2 · Cited by 11
“Iron-sulfur (Fe-S) proteins serve a wide variety of essential tasks in living systems, including electron transfer within and between proteins, catalysis of chemical reactions, sensing the chemical environment, regulation of DNA expression, repair of damaged DNA, and maintenance of molecular structure [1].”
BackgroundDual functions of NifEN: insights into the evolution and mechanism of nitrogenase
Hu, Y., Fay, A. W., Lee, C. C., Wiig, J. A., & Ribbe, M. W. (2010) · Dalton Transactions · doi:10.1039/b922555b · Cited by 12
Functional role of metalloproteins in genome stability
Zhang, C., Zhang, F., Zhou, P., & Zhang, C. (2016) · Frontiers in Biology · doi:10.1007/s11515-016-1392-4 · Cited by 10
Zhang, P., Liu, Y., Wang, M., Dong, M., Liu, Z., Jia, Z., Wang, W., Zhang, A., Wang, L., & Song, L. (2018) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2018.03.007 · Cited by 11
Generation of 34S-substituted protein-bound [4Fe-4S] clusters using 34S-L-cysteine
Crack, J. C., Stewart, M. Y., & Brun, N. E. L. (2018) · Biology Methods and Protocols · doi:10.1093/biomethods/bpy015 · Cited by 11
“arrangements that differ in nuclearity as well as shape, for example, the rhombic [2Fe-2S] and cubic [4Fe-4S] clusters [1].”
BackgroundMcGuinness, E. T. (2010) · Chemical Reviews · doi:10.1021/cr050061l · Cited by 11
Bolstad, H. M., & Wood, M. J. A. (2010) · Journal of Proteome Research · doi:10.1021/pr100920r · Cited by 11
Cluster and Fold Stability of E. coli ISC-Type Ferredoxin
Yan, R., Adinolfi, S., Iannuzzi, C., Kelly, G. P., Oregioni, A., Martin, S. R., & Pastore, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078948 · Cited by 11
“This high oxygen sensitivity is shared, in the ISC operon, also by the scaffold protein IscU and is probably related to the necessity of this machine to be highly sensitive to oxidative stress [1,2,3].”
BackgroundSNAP‐25 is also an iron–sulfur protein
Huang, Q., Hong, X., & Hao, Q. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.028 · Cited by 11
“Another interesting question is: what is the biological function of the SNAP-25a containing an iron–sulfur cluster, or what is the biological function of the iron–sulfur cluster itself? The iron–sulfur cluster is the most ancient, ubiquitous, and structurally and functionally diverse prosthetic group of proteins [23,2…”
BackgroundWang, Y., Lee, J., & Ding, H. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.05.007 · Cited by 11
“Iron-sulfur proteins are involved in diverse physiological functions ranging from energy metabolism to DNA replication and repair [1].”
Tong, T., Zhou, Y., Fei, F., Zhou, X., Guo, Z., Wang, S., Zhang, J., Zhang, P., Cai, T., Li, G., et al. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1051943 · Cited by 9
“Later, a wide variety of biological functions have emerged for these clusters, including nitrogen fixation, DNA replication and repair (Kiley and Beinert, 2003; Johnson et al., 2005; Fontecave, 2006; Mettert and Kiley, 2015; Rouault, 2015).”
BackgroundResearch progress on the biosynthesis and delivery of iron–sulfur clusters in the plastid
Yang, B., Xu, C., Cheng, Y., Jia, T., & Hu, X. (2023) · Plant Cell Reports · doi:10.1007/s00299-023-03024-7 · Cited by 10
“To date, genetic and biochemical studies have revealed three distinct systems responsible for Fe–S cluster biosynthesis, termed NIF (nitrogen fixation), ISC (iron–sulfur cluster) and SUF (sulfur utilization factor) (Johnson et al. 2005).”
BackgroundSolubilization of elemental sulfur by surfactants promotes reduction to H 2 S by thiols
Garcia, A. C., & Pluth, M. D. (2023) · Chemical Communications · doi:10.1039/d3cc01914d · Cited by 10
Saini, J., Deere, T. M., & Lessner, D. J. (2023) · Scientific Reports · doi:10.1038/s41598-023-42400-x · Cited by 10
WhiB-like proteins: Diversity of structure, function and mechanism
Beltran, D. G., Wan, T., & Zhang, L. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119787 · Cited by 10
Mitochondrial glutaredoxin Grx5 functions as a central hub for cellular iron-sulfur cluster assembly
Pandey, A. K., Pain, J., Singh, P., Dancis, A., & Pain, D. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108391 · Cited by 10
“Fe-S proteins play vital roles in fundamental cellular processes, including respiration, enzyme catalysis, DNA synthesis and repair, tRNA modi fi cations, protein translation, and sensing of intracellular oxygen or iron levels (17 – 19).”
Localized Active Space State Interaction Singles
Hermes, M. R., Jangid, B., Agarawal, V., & Gagliardi, L. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c00387 · Cited by 10
Tzeli, D., Raugei, S., & Xantheas, S. S. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c00485 · Cited by 10
Shomar, H., & Bokinsky, G. (2021) · Molecules · doi:10.3390/molecules26226930 · Cited by 10
Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease
Karunakaran, G., Yang, Y., Tremblay, V., Ning, Z., Martin, J., Belaouad, A., Figeys, D., Brunzelle, J. S., Giguère, P. M., Stintzi, A. P., et al. (2022) · FEBS Letters · doi:10.1002/1873-3468.14295 · Cited by 10
Dey, A., Albert, T., Kong, R. Y., MacMillan, S. N., Moënne‐Loccoz, P., Lancaster, K. M., & Goldberg, D. P. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.2c02383 · Cited by 10
Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster
Rutledge, H. L., Field, M. J., Rittle, J., Green, M. T., & Tezcan, F. A. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c09480 · Cited by 10
Zars, E., Gravogl, L., Gau, M. R., Carroll, P. J., Meyer, K., & Mindiola, D. J. (2023) · Chemical Science · doi:10.1039/d3sc01094e · Cited by 10
Mikhlin, Y. L., Борисов, Р. В., Likhatski, M., Bayukov, O. A., Knyazev, Y. V., Zharkov, S. M., Vorobyev, S., Tomashevich, Y. V., Ivaneeva, A. D., Karacharov, A. A., et al. (2023) · New Journal of Chemistry · doi:10.1039/d3nj00758h · Cited by 10
Insights into the structure of the diiron site of RIC from Escherichia coli
Nobre, L. S., Lousa, D., Pacheco, I., Soares, C. M., Teixeira, M. S., & Saraiva, L. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2014.12.028 · Cited by 10
“Repair of Iron Centres (RIC) proteins are diiron-containing proteins that protect iron–sulphur (Fe–S) enzymes from damage inflicted by oxidative and nitrosative stresses [1].”
BackgroundBiogenesis of [Fe–S] cluster in Firmicutes: an unexploited field of investigation
Riboldi, G. P., de Mattos, E. P., & Jeverson Frazzon, B. (2013) · Antonie van Leeuwenhoek · doi:10.1007/s10482-013-9966-5 · Cited by 10
“Interestingly, no amino acid sequence has been identified as a putative binding motif for [Fe–S] clusters (Johnson et al. 2005).”
BackgroundA three-dimensional topology of complex I inferred from evolutionary correlations
Kensche, P. R., Duarte, I., & Huynen, M. A. (2012) · BMC Structural Biology · doi:10.1186/1472-6807-12-19 · Cited by 10
“Although the cysteines are not fully conserved, occasionally FeS-clusters are bound by serine, histidine, or aspartate [71].”
BackgroundHybrid Methods in Iron-Sulfur Cluster Biogenesis
Prischi, F., & Pastore, A. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00012 · Cited by 10
“…prosthetic groups involved in a multitude of biological functions, such as electron transfer, gene expression regulation, thiolation, photosynthesis, nitrogen fixation, metal trafficking, substrate binding, DNA repair/replication and RNA modification (Johnson et al., 2005; Mettert and Kiley, 2015).”
BackgroundS-Adenosylmethionine Metabolism and Aging
Loenen, W. A. M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811060-7.00003-6 · Cited by 11
Lee, E. D., Navas, K. I., & Portnoy, D. A. (2019) · Infection and Immunity · doi:10.1128/iai.00788-19 · Cited by 10
“Three distinct pathways for FeS cluster synthesis have been identified and designated the Nif, Suf, and Isc systems (31).”
BackgroundSatyanarayan, M. B., Zhao, J. Y., Zhang, J., Yu, F., & Lu, Y. (2021) · Plant Direct · doi:10.1002/pld3.303 · Cited by 10
Fonseca, J. P., Oh, S., Boschiero, C., Watson, B. S., Huhman, D. V., & Mysore, K. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137147 · Cited by 10
Xie, Z.-X., Yan, K., Kong, L., Gai, Y., Jin, T., He, Y., Wang, Y., Chen, F., Lin, L., Lin, Z., et al. (2022) · Marine Life Science & Technology · doi:10.1007/s42995-021-00119-6 · Cited by 10
“For nitrogen metabolism, NifU (K04488), a scaffold protein destined for nitrogenase maturation (Johnson et al. 2005), was more abundant at high-temperature sites, suggesting that nitrogen fixation activity might be linked to temperature.”
BackgroundPlant pathogenic bacterium can rapidly evolve tolerance to an antimicrobial plant allelochemical
Alderley, C. L., Greenrod, S. T. E., & Friman, V. (2022) · Evolutionary Applications · doi:10.1111/eva.13363 · Cited by 10
“Iron-sulfur clusters have been implicated in cellular metabolism, protein structural stabilisation, iron storage, and the regulation of gene expression (Johnson et al., 2005).”
BackgroundZhang, T., Zhang, A., Bell, S. G., Wong, L., & Zhou, W. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s139900471400474x · Cited by 10
Ouyang, J., Liu, Q., Li, B., Ao, J., & Chen, X. (2012) · Indian Journal of Microbiology · doi:10.1007/s12088-012-0322-7 · Cited by 10
“This intermediate can then open the S8 ring [20, 21].”
Jaroschinsky, M., Pinske, C., & Sawers, R. G. (2017) · Microbiology · doi:10.1099/mic.0.000481 · Cited by 10
“Radical SAM enzymes belong to an ancient family of FeS enzymes with roles in anaerobic DNA synthesis, cofactor biosynthesis and formate metabolism [2].”
BackgroundInfluentialBouchard, S., Bruschi, M., GIOIA, L. D., Roy, C. L., Pétillon, F. Y., Schollhammer, P., & Talarmin, J. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b02861 · Cited by 10
Kubas, A. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c00126 · Cited by 9
Corrins and porphyrins: two of nature’s pigments of life
Marques, H. M. (2024) · Journal of Coordination Chemistry · doi:10.1080/00958972.2024.2343109 · Cited by 13
Terahata, T., Shimada, Y., Maki, C., Muroga, S., Sakurai, R., Kunichika, K., & Fujishiro, T. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c02654 · Cited by 9
Iron-sulfur cluster proteins present the weak spot in non-thermal plasma-treated Escherichia coli
Krewing, M., Weisgerber, K. M., Dirks, T., Bobkov, I., Schubert, B., & Bandow, J. E. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103562 · Cited by 9
“In E. coli , [FeS] clusters are synthesized either by the isc or the suf pathway [24].”
Zhang, B., Xiu, X.-L., Chen, L., Sui, X. Y., Zheng, R., Guo, Y., Cai, X., Liu, Z., & Zheng, Y. (2025) · Green Chemistry · doi:10.1039/d5gc00433k · Cited by 9
Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli
Ding, H. (2025) · Metallomics · doi:10.1093/mtomcs/mfaf040 · Cited by 8
“Iron-sulfur proteins have been discovered in diverse physiological processes ranging from energy metabolism to DNA replication and repair [ 1 ].”
Lee, Y., Abboud, K. A., García‐Serres, R., & Murray, L. J. (2016) · Chemical Communications · doi:10.1039/c6cc04671a · Cited by 9
Cheng, F., Zhao, B., Jiang, B., Lu, Y., Li, W., Jin, B., & Wang, L. (2018) · Plant Signaling & Behavior · doi:10.1080/15592324.2018.1550316 · Cited by 9
Ren, Y., Eronen, V., Andberg, M. B., Koivula, A., & Hakulinen, N. (2022) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-022-02252-5 · Cited by 9
“The [Fe–S] clusters are evolutionarily ancient prosthetic groups found in many metabolically important enzymes, and are suggested to participate in electron transfer and iron–sulphur storage, catalysis, regulation of gene expression, and in oligomer formation [70].”
BackgroundZhang, S., Ke, C., Jiang, M., Li, Y., Huang, W., Dang, Z., & Guo, C. (2023) · Environmental Pollution · doi:10.1016/j.envpol.2023.121516 · Cited by 9
Mrp and SufT, Two Bacterial Homologs of Eukaryotic CIA Factors Involved in Fe-S Clusters Biogenesis
Aubert, C., Mandin, P., & Py, B. (2023) · Inorganics · doi:10.3390/inorganics11110431 · Cited by 10
“Other types of clusters, albeit less frequent, are cubic [3Fe-4S] clusters that for instance arise from the degradation of a [4Fe-4S] cluster, linear [3Fe-4S] clusters, or even more complex clusters, such as the H-cluster in hydrogenase and the P-cluster and FeMo-cofactor in nitrogenase [3,9].”
BackgroundWachnowsky, C., Hendricks, A. L., Wesley, N. A., Ferguson, C., Fidai, I., & Cowan, J. A. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01278 · Cited by 10
Mintmier, B., Nassif, S., Stolz, J. F., & Basu, P. (2020) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-020-01787-y · Cited by 10
Xiang, G., Fu, Q., Li, G., Liu, R., Liu, G., Yin, X., Chen, T., & Xu, Y. F. (2022) · Molecular Plant Pathology · doi:10.1111/mpp.13266 · Cited by 9
Coronado, E., Roggo, C., & van der Meer, J. R. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00585 · Cited by 9
“Proteins containing iron-sulfur clusters participate in a diversity of functions such as electron transport, substrate binding, regulation of gene expression and enzymatic activities (Johnson et al., 2005).”
Che, L., Gardenghi, D. J., Szilagyi, R. K., & Minton, T. K. (2011) · Langmuir · doi:10.1021/la2002833 · Cited by 9
Mechanistic Aspects of Redox‐Induced Assembly and Disassembly of S‐Bridged [2M‐2S] Structures
Koch, F., Berkefeld, A., Speiser, B., & Schubert, H. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201704599 · Cited by 9
Morozov, G. I., Porat, N., Kushnir, T., Najmuldeen, H. H. R., Adawi, A., Caspi, V. C., Benisty, R., Ohayon, A., Liron, O., Azriel, S., et al. (2018) · Scientific Reports · doi:10.1038/s41598-017-18645-8 · Cited by 9
The Active Site of Nitrile Hydratase: An Assembly of Unusual Coordination Features by Nature
Mascharak, P. K. (2013) · Structure and bonding · doi:10.1007/430_2012_85 · Cited by 9
“Fe-SCys ligation is quite common in iron proteins such as ferredoxins [28] and cytochrome P450 family [29]; in most cases, such bonds do not require further oxygenation for catalytic activity.”
BackgroundWesley, N. A., Wachnowsky, C., Fidai, I., & Cowan, J. A. (2017) · FEBS Journal · doi:10.1111/febs.14270 · Cited by 9
Carbon Monoxide and Cyanide Ligands in the Active Site of [FeFe]-Hydrogenases
Peters, J. W. (2009) · Royal Society of Chemistry eBooks · doi:10.1039/9781847559333-00179 · Cited by 9
The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein
Quist, T., Chen, J., MacNeil, A., & Pandelia, M. (2023) · Inorganics · doi:10.3390/inorganics11120475 · Cited by 8
“…are remarkably multifunctional, and in addition to their ability to exchange electrons, they also serve as structural elements, catalytic centers, small molecule sensors (i.e., O 2 , NO) and donors (i.e., iron and sulfide), and electron carriers to or recruiters of nucleic acids [2,3,6–10].”
Kairis, A., Neves, B. D., Couturier, J., Remacle, C., & Rouhier, N. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119797 · Cited by 9
A naturalist perspective of microbiology: Examples from methanogenic archaea
Boyd, E. S., Spietz, R. L., Kour, M., & Colman, D. R. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16285 · Cited by 7
Saghaug, C. S., Gamlem, A. L., Hauge, K. B., Vahokoski, J., Klotz, C., Aebischer, T., Langeland, N., & Hanevik, K. (2022) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2022.12.003 · Cited by 8
“The fd domain contains cysteine residues with iron-sulfur (Fe–S) cluster forming abilities which are part of redox-active centers responsible for biological electron transport (Johnson et al., 2005; Ansell et al., 2017).”
BackgroundCysB Is a Key Regulator of the Antifungal Activity of Burkholderia pyrrocinia JK-SH007
Yu, M., Tang, Y., Lu, L.-X., Kong, W., & Ye, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098067 · Cited by 8
“In addition, Bp_007_sr4 is upregulated after CysB is disrupted, and it mainly targets cysteine desulfurase, which is required for Fe–S cluster biosynthesis [40].”
Zahn, L. E., Gannon, P. M., & Rajakovich, L. J. (2024) · Metallomics · doi:10.1093/mtomcs/mfae049 · Cited by 9
Prebiotic synthesis of the major classes of iron–sulfur clusters
Scintilla, S., Rossetto, D., Clémancey, M., Rendon, J., Ranieri, A., Guella, G., Assfalg, M., Borsari, M., Gambarelli, S., Blondin, G., et al. (2025) · Chemical Science · doi:10.1039/d5sc00524h · Cited by 8
Lights on Iron-Sulfur Clusters
Lillig, C. H., & Lill, R. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.12.005 · Cited by 8
“…distinct steps during the de novo biosynthesis of the Fe/S clusters and their insertion into apoproteins (Fontecave and Ollagnier-de-Choudens, 2008; Johnson et al., 2005; Lill, 2009), and functional characterization of the key components enabled elucidation of some basic biogenesis principles.”
BackgroundFluor‐, Amino‐ und Thiolinhibitoren im Komplex mit dem [Fe4S4]‐Protein IspH
Span, I., Wang, K., Wang, W., Jauch, J., Eisenreich, W., Bacher, A., Oldfield, E., & Groll, M. (2013) · Angewandte Chemie · doi:10.1002/ange.201208469 · Cited by 8
Redox Proteins as Targets for Drugs Development Against Pathogens
Catalano‐Dupuy, D. L., Rivero, A. S. L., Soldano, A., & Ceccarelli, E. A. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319140009 · Cited by 8
“The SufB, SufC, and SufD proteins are associated as a stable complex, and SufC has been shown to display ATPase activity [135,137].”
BackgroundInfluentialHemerythrin is required for Aeromonas hydraphlia to survive in the macrophages of Anguilla japonica
Zeng, W., Chen, W. B., Yan, Q., Lin, G. F., & Qin, Y. (2016) · Genetics and Molecular Research · doi:10.4238/gmr.15028074 · Cited by 8
Lu, H., Li, J.-D., Zhang, Y.-D., Lü, X.-L., Xu, C., Huang, Y., & Gribskov, M. (2020) · Genome Biology and Evolution · doi:10.1093/gbe/evaa038 · Cited by 8
Spin-symmetrised structures and vibrational frequencies of iron–sulfur clusters
Cappelluti, F., Bencivenni, L., & Guidoni, L. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/d0cp01591a · Cited by 8
Correlation between Charge Transport and Base Excision Repair in the MutY–DNA Glycosylase
Teo, R. D., Du, X., Vera, H. L. T., Migliore, A., & Beratan, D. N. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c08598 · Cited by 8
The ataxia-telangiectasia mutated gene product regulates the cellular acid-labile sulfide fraction
Islam, M. Z., Shen, X., Pardue, S., Kevil, C. G., & Shackelford, R. E. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103344 · Cited by 8
Peña‐Diaz, P., Braymer, J. J., Vacek, V., Zelená, M., Lometto, S., Mais, C.-N., Hrdý, I., Treitli, S. C., Hochberg, G. K. A., Py, B., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.07.018 · Cited by 8
All-Ferrous Iron–Sulfur Clusters
Yao, W., Gurubasavaraj, P. M., & Holland, P. L. (2012) · Structure and bonding · doi:10.1007/430_2012_81 · Cited by 9
Mühlenhoff, U., Molik, S., Godoy, J. R., Uzarska, M. A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.09.007 · Cited by 8
Theoretical Insights into the Unique Ligation of [Fe4S4] Iron–Sulfur Clusters
Kubas, A., & Maszota, P. (2018) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201800165 · Cited by 8
Identification of a nth-Like Gene Encoding an Endonuclease III in Campylobacter jejuni
Dai, L., Xia, J., Şahin, O., & Zhang, Q. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00698 · Cited by 9
“jejuni Cj1083c lacks an iron/sulfur cluster region, which was proposed to have a structural role for the DNA repair (Guan et al., 1998; Johnson et al., 2005).”
BackgroundMiyagawa, K., Shoji, M., Isobe, H., Yamanaka, S., Kawakami, T., Okumura, M., & Yamaguchi, K. (2020) · Molecular Physics · doi:10.1080/00268976.2020.1760388 · Cited by 8
The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]2+ cluster in vivo
Rosenbach, H., Walla, E., Cutsail, G. E., Birrell, J. A., Pascual-Ortiz, M., DeBeer, S., Fleig, U. N., & Span, I. (2021) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-020-01840-w · Cited by 8
“Fe–S clusters occur in nature in different shapes and nuclearities, and the most common types are the rhombic [2Fe-2S] cluster and the cubic [4Fe-4S] cluster [2].”
BackgroundLow reduction potential cytochrome b5 isotypes of Giardia intestinalis
Pazdzior, R., Yang, Z., Mesbahuddin, M. S., Yee, J., van der Est, A., & Rafferty, S. P. (2015) · Experimental Parasitology · doi:10.1016/j.exppara.2015.08.004 · Cited by 6
Montejano-Ramírez, V., Martínez-Cámara, R., García‐Pineda, E., & Valencia‐Cantero, E. (2018) · Acta Physiologiae Plantarum · doi:10.1007/s11738-018-2712-x · Cited by 8
Rao, G., Alwan, K. B., Blackburn, N. J., & Britt, R. D. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01293 · Cited by 8
Lee, K., Booker, S. J., Cicchillo, R. M., Grove, T. L., & Nesbitt, N. M. (2008) · Oxidative stress and disease · doi:10.1201/9781420045390.ch2 · Cited by 8
Sodium thiosulfate: A donor or carrier signaling molecule for hydrogen sulfide?
Tang, S.-M., Lu, G., Lei, X., Yang, X., Tang, G., Yu, J., & Xie, Z.-Z. (2024) · Nitric Oxide · doi:10.1016/j.niox.2024.06.004 · Cited by 7
Meta-analysis Driven Strain Design for Mitigating Oxidative Stresses Important in Biomanufacturing
Phaneuf, P. V., Kim, S. H., Rychel, K., Rode, C., Beulig, F., Palsson, B. Ø., & Yang, L. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00572 · Cited by 6
“13,14 19 − 25 It has also been observed that ALE-generated mutations are not frequently observed in natural isolates, 26 highlighting their distinctiveness.”
BackgroundGrossman, J. D., Camire, E. J., & Perlstein, D. L. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.11.005 · Cited by 7
Stewart, J. A., & Bhagwat, A. S. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103381 · Cited by 7
Metalloproteins and the Pyrite-based Origin of Life: A Critical Assessment
Rivas, M., Becerra, A., Peretó, J. G., Bada, J. L., & Lazcano, A. (2011) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-011-9238-1 · Cited by 8
“Due to their electron transfer properties, they play a major role in bioenergetic processes, catalysis and regulation, and are involved in iron/sulfur storage, and regulation of gene expression processes involved in the response to oxidative stress and photosynthetic and respiratory processes ( Johnson et al. 2005 ; M…”
BackgroundBarborini, M., & Guidoni, L. (2016) · The Journal of Chemical Physics · doi:10.1063/1.4963015 · Cited by 7
Mao, Z., Carroll, E. C., Kim, P. W., Cramer, S. P., & Larsen, D. S. (2017) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.7b02026 · Cited by 7
A missed Fe-S cluster handoff causes a metabolic shakeup
Berteau, O. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.h118.002883 · Cited by 7
“vinelandii, a model organism for [Fe-S] cluster biogenesis (1).”
Background
Metadata
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review