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

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1146/annurev.biochem.74.082803.133518

Cites

209 of 209 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891
DNA Microarray-Mediated Transcriptional Profiling of the Escherichia coli Response to Hydrogen Peroxide
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

Show all 209 references

Research works printed but not linked: 4

Johnson MK. 1994. InEncyclopedia of Inorganic Chemistry, ed.RB King, pp.1896–915. Chichester, UK: Wiley
Thauer RK, Schonheit P. 1982. InIron-Sulfur Proteins, ed.TG Spiro, pp.329–41. New York: Wiley
10.1074/jbc.275.12.8283 · DOI
10.1074/jbc.M104067200 · DOI

Sorted by citations

Items 201–300 of 1,000

The Asymmetric Trimeric Architecture of [2Fe–2S] IscU: Implications for Its Scaffolding during Iron–Sulfur Cluster Biosynthesis
Shimomura, Y., Wada, K., Fukuyama, K., & Takahashi, Y. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.015 · Cited by 106
Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions
Marsh, E. N. G., Patterson, D. P., & Li, L. (2010) · ChemBioChem · doi:10.1002/cbic.200900777 · Cited by 104
A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation
Netz, D. J. A., Pierik, A. J., Stümpfig, M., Bill, E., Sharma, A. K., Pallesen, L. J., Walden, W. E., & Lill, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328914 · Cited by 106
“The ability to assemble and deliver Fe-S clusters both in vivo and in vitro support a scaffold role for Cfd1 andNbp35, suggesting that their functionmay be similar to the mitochondrial Isu1 and bacterial IscU scaffold proteins of the ISC assembly systems (3, 8).”
Background
An Iron-Sulfur Cluster Is Essential for the Binding of Broken DNA by AddAB-type Helicase-Nucleases
Yeeles, J. T. P., Cammack, R., & Dillingham, M. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808526200 · Cited by 105
Copper binding in IscA inhibits iron‐sulphur cluster assembly in E scherichia coli
Tan, G., Cheng, Z., Pang, Y., Landry, A. P., Li, J., Lu, J., & Ding, H. (2014) · Molecular Microbiology · doi:10.1111/mmi.12676 · Cited by 103
“Since iron-sulphur proteins are involved in diverse physiological processes from energy metabolism to DNA repair and replication (Johnson et al., 2005; White and Dillingham, 2012), the copper-mediated inhibition of iron-sulphur cluster biogenesis would have a broad impact on multiple cellular…”
Background
Mitochondrial dysfunction promotes aquaporin expression that controls hydrogen peroxide permeability and ferroptosis
Takashi, Y., Tomita, K., Kuwahara, Y., Roudkenar, M. H., Roushandeh, A. M., Igarashi, K., Nagasawa, T., Nishitani, Y., & Sato, T. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.027 · Cited by 104
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103
Metallocenter assembly of the hydrogenase enzymes
Leach, M. R., & Zamble, D. B. (2007) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.01.011 · Cited by 104
In vitro synthesis of the iron–molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins
Curatti, L., Hernández, J. A., Igarashi, R. Y., Soboh, B., Zhao, D., & Rubio, L. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703050104 · Cited by 104
Clinical manifestation and a new ISCU mutation in iron–sulphur cluster deficiency myopathy
Kollberg, G., Tulinius, M., Melberg, A., Darín, N., Andersen, O., Holmgren, D., Oldfors, A., & Holme, E. (2009) · Brain · doi:10.1093/brain/awp152 · Cited by 106
“S clustering formation and transfer have come from studies on Escherichia coli and yeast (Johnson et al., 2005).”
Background
Mitochondrial iron metabolism and its role in diseases
Gao, J., Zhou, Q., Wu, D., & Chen, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.12.005 · Cited by 111
Iron–Sulfur Clusters: Biogenesis, Molecular Mechanisms, and Their Functional Significance
Xu, X. M., & Møller, S. G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3259 · Cited by 102
“…through nucleophilic attack by the thiolate anion of the active-site cysteine on the sulfur of the substrate L-cysteine and alanine release, and (iii) subsequent transfer of substrate-derived sulfur of the cysteine persulﬁde residue to different biomol-ecules such as [Fe-S] scaffolds (25, 130).”
Influential
Studies on the Mechanism of Catalysis of Iron−Sulfur Cluster Transfer from IscU[2Fe2S] by HscA/HscB Chaperones
Bonomi, F., Iametti, S., Morleo, A., Ta, D. T., & Vickery, L. E. (2008) · Biochemistry · doi:10.1021/bi801565j · Cited by 101
“Figures showing (1) the binding of IscU to HscA(T212V) monitored by isothermal titration calorimetry and (2) the effect of ATP on the absorption spectrum of HscA(T212V).”
Native Escherichia coli SufA, Coexpressed with SufBCDSE, Purifies as a [2Fe−2S] Protein and Acts as an Fe−S Transporter to Fe−S Target Enzymes
Gupta, V., Sendra, M., Naik, S., Chahal, H. K., Huynh, B. H., Outten, F. W., Fontecave, M., & de Choudens, S. O. (2009) · Journal of the American Chemical Society · doi:10.1021/ja807551e · Cited by 101
Protonation/reduction dynamics at the [4Fe–4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases
Senger, M., Mebs, S., Duan, J., Shulenina, O. V., Laun, K., Kertess, L., Wittkamp, F., Apfel, U., Happe, T., Winkler, M., et al. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp04757f · Cited by 100
The Torpid State: Recent Advances in Metabolic Adaptations and Protective Mechanisms†
Giroud, S., Habold, C., Nespolo, R. F., Mejías, C., Terrien, J., Logan, S. M., Henning, R. H., & Storey, K. B. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.623665 · Cited by 100
Widespread Distribution in Pathogenic Bacteria of Di-Iron Proteins That Repair Oxidative and Nitrosative Damage to Iron-Sulfur Centers
Overton, T. W., Justino, M. C., Li, Y., Baptista, J. M., Melo, A. M. P., Cole, J. A., & Saraiva, L. M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01733-07 · Cited by 100
“Specialized systems have evolved that facilitate the assembly and insertion of Fe-S clusters into proteins, namely, the products of isc, suf, and csd operons (12, 13, 21).”
Background
Structure and Dynamics of the Iron−Sulfur Cluster Assembly Scaffold Protein IscU and Its Interaction with the Cochaperone HscB
Kim, J. H., Füzéry, A. K., Tonelli, M., Ta, D. T., Westler, W. M., Vickery, L. E., & Markley, J. L. (2009) · Biochemistry · doi:10.1021/bi9002277 · Cited by 99
Identifying cysteines and histidines in transition‐metal‐binding sites using support vector machines and neural networks
Passerini, A., Punta, M., Ceroni, A., Rost, B., & Frasconi, P. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21135 · Cited by 100
“For each target residue, we computed the sequence separation to the following target if any and discretized such a value into eight bins ([1, 1], [2, 2], [3, 3], [4, 4], [5, 6], [7, 20], [21, 75], [76, 200] [201, ?”
Method
Transcriptional analysis of Clostridium beijerinckii NCIMB 8052 to elucidate role of furfural stress during acetone butanol ethanol fermentation
Zhang, Y., & Ezeji, T. C. (2013) · Biotechnology for Biofuels · doi:10.1186/1754-6834-6-66 · Cited by 98
“Notably, the iron-sulfur cluster plays important roles in electron transfer by redox enzymes, disulfide reduction by ferredoxin:thioredoxin reductase, regulation of gene expressions associated with Ferredoxin-NADP reductase, and iron and sulfur storage in ferredoxins [24].”
Background
AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis
Xu, X. M., & Møller, S. G. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600968 · Cited by 97
“S cluster biogenesis is divided into elemental sulfur formation, iron acquisition, assembly of sulfur and iron into a cluster, and cluster insertion into apoproteins (Johnson et al, 2005; Lill and Muhlenhoff, 2005).”
Background
Roles of the Mammalian Cytosolic Cysteine Desulfurase, ISCS, and Scaffold Protein, ISCU, in Iron-Sulfur Cluster Assembly
Li, K., Tong, W.-H., Hughes, R. M., & Rouault, T. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600582200 · Cited by 97
Effector Role Reversal during Evolution: The Case of Frataxin in Fe–S Cluster Biosynthesis
Bridwell‐Rabb, J., Iannuzzi, C., Pastore, A., & Barondeau, D. P. (2012) · Biochemistry · doi:10.1021/bi201628j · Cited by 96
Iron–sulfur cluster biosynthesis and trafficking – impact on human disease conditions
Wachnowsky, C., Fidai, I., & Cowan, J. A. (2017) · Metallomics · doi:10.1039/c7mt00180k · Cited by 99
Evolution of Mitochondrial Chaperones Utilized in Fe-S Cluster Biogenesis
Schilke, B. A., Williams, B. L., Knieszner, H., Pukszta, S., D’Silva, P., Craig, E. A., & Marszałek, J. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.069 · Cited by 96
“Biogenesis of Fe-S clusters is an essential process [1].”
Biomimetic Chemistry of Iron, Nickel, Molybdenum, and Tungsten in Sulfur-Ligated Protein Sites
Groysman, S., & Holm, R. H. (2009) · Biochemistry · doi:10.1021/bi900044e · Cited by 98
Analysis of iron–sulfur protein maturation in eukaryotes
Pierik, A. J., Netz, D. J. A., & Lill, R. (2009) · Nature Protocols · doi:10.1038/nprot.2009.39 · Cited by 94
“Despite the chemical simplicity of Fe/S clusters, their biosynthesis and insertion into apoproteins within cells require dedicated and complex machiner”
Background
ProP Is Required for the Survival of Desiccated Salmonella enterica Serovar Typhimurium Cells on a Stainless Steel Surface
Finn, S., Händler, K., Condell, O., Colgan, A. M., Cooney, S., Mcclure, P. J., zquita, A. ⁄. J. A. ⁄., Hinton, J. C. D., & Fanning, S. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.00515-13 · Cited by 95
“A number of genes involved in the formation of Fe-S clusters (including iscA, iscS, and fdx), as well as the manganese superoxide dismutase gene sodA, which are induced under iron-limiting conditions (37, 38), were also upregulated.”
Background
Frataxin Directly Stimulates Mitochondrial Cysteine Desulfurase by Exposing Substrate-binding Sites, and a Mutant Fe-S Cluster Scaffold Protein with Frataxin-bypassing Ability Acts Similarly
Pandey, A., Gordon, D. M., Pain, J., Stemmler, T. L., Dancis, A., & Pain, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525857 · Cited by 94
“The enzymatic cycle of cysteine desulfurase includes formation of a covalent persulfide on the active site cysteine (21, 27, 32, 33).”
Background
Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis
Hirabayashi, K., Yuda, E., Tanaka, N., Katayama, S., Iwasaki, K., Matsumoto, T., Kurisu, G., Outten, F. W., Fukuyama, K., Takahashi, Y., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680934 · Cited by 94
“In eukaryotes, including mammalian cells, the ISC system (59) and its dependent CIA system (60) are responsible for nascent Fe-S cluster biogenesis.”
Background
Change Is Good: Variations in Common Biological Mechanisms in the Epsilonproteobacterial GeneraCampylobacterandHelicobacter
Gilbreath, J. J., Cody, W. L., Merrell, D. S., & Hendrixson, D. R. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00035-10 · Cited by 94
Monothiol Glutaredoxins Function in Storing and Transporting [Fe2S2] Clusters Assembled on IscU Scaffold Proteins
Shakamuri, P., Zhang, B., & Johnson, M. K. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306061x · Cited by 95
The Origin and Evolution of Ribonucleotide Reduction
Lundin, D., Berggren, G., Logan, D. T., & Sjöberg, B. (2015) · Life · doi:10.3390/life5010604 · Cited by 106
“, AdoCbl) requires complex machineries in modern organisms [22,23], iron-sulfur clusters can form spontaneously in vitro from relatively simple starting materials [24,25] and abiotic porphyrin synthesis has been suggested [26].”
Background
A role for tetrahydrofolates in the metabolism of iron-sulfur clusters in all domains of life
Waller, J. C., Alvarez, S., Naponelli, V., Lara‐Núñez, A., Blaby, I. K., Silva, V. D., Ziemak, M. J., Vickers, T. J., Beverley, S. M., Edison, A. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911586107 · Cited by 93
“The cDNA was cloned into the NcoI and XbaI sites of pBAD24 (1), excised with NcoI and SalI, and cloned into pET-28bðþÞ (Novagen).”
Method
O2 Reactions at the Six-iron Active Site (H-cluster) in [FeFe]-Hydrogenase
Lambertz, C., Leidel, N., Havelius, K. G. V., Noth, J., Chernev, P., Winkler, M., Happe, T., & Haumann, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.283648 · Cited by 93
CpSufE Activates the Cysteine Desulfurase CpNifS for Chloroplastic Fe-S Cluster Formation
Ye, H., Abdel‐Ghany, S. E., Anderson, T. D., Pilon‐Smits, E. A. H., & Pilon, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512737200 · Cited by 93
Cysteine Depletion Causes Oxidative Stress and Triggers Outer Membrane Vesicle Release by Neisseria meningitidis; Implications for Vaccine Development
van de Waterbeemd, B., Zomer, G., van den IJssel, J., van Keulen, L., Eppink, M. H. M., van der Ley, P., & van der Pol, L. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054314 · Cited by 92
“[50,51].”
Mechanism of activation of the human cysteine desulfurase complex by frataxin
Patra, S., & Barondeau, D. P. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909535116 · Cited by 90
“Fe-S clusters are protein cofactors that are necessary for many critical biochemical processes (9, 10).”
Background
Ferredoxin Competes with Bacterial Frataxin in Binding to the Desulfurase IscS*
Yan, R., Konarev, P. V., Iannuzzi, C., Adinolfi, S., Roche, B., Kelly, G. P., Simon, L., Martin, S. R., Py, B., Barras, F., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.480327 · Cited by 92
“Fe-S cluster proteins are ubiquitous and perform a variety of roles including electron transfer, enzyme regulation, and regulation of gene expression (1, 2).”
Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis
Uhrigshardt, H., Singh, A., Kovtunovych, G., Ghosh, M. C., & Rouault, T. A. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq301 · Cited by 93
Revisiting the IspH Catalytic System in the Deoxyxylulose Phosphate Pathway: Achieving High Activity
Xiao, Y., Chu, L., Sanakis, Y., & Liu, P. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903778d · Cited by 91
X-ray Structure of the Complete ABC Enzyme ABCE1 from Pyrococcus abyssi
Kärcher, A., Schele, A., & Hopfner, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707347200 · Cited by 91
Spectroscopic and Functional Characterization of Iron–Sulfur Cluster-Bound Forms of Azotobacter vinelandii Nif IscA
Mapolelo, D. T., Zhang, B., Naik, S., Huynh, B. H., & Johnson, M. K. (2012) · Biochemistry · doi:10.1021/bi3006658 · Cited by 90
Complementary roles of SufA and IscA in the biogenesis of iron–sulfur clusters in Escherichia coli
Lü, J., Yang, J., Tan, G., & Ding, H. (2007) · Biochemical Journal · doi:10.1042/bj20071166 · Cited by 90
Controlled Expression of nif and isc Iron-Sulfur Protein Maturation Components Reveals Target Specificity and Limited Functional Replacement between the Two Systems
Santos, P. C. D., Johnson, D. C., Ragle, B. E., Unciuleac, M.-C., & Dean, D. R. (2007) · Journal of Bacteriology · doi:10.1128/jb.01734-06 · Cited by 90
“In spite of their simple composition and architecture, the biological formation of [Fe-S] clusters is surprisingly complex (3, 15).”
Background
X-ray Absorption and Emission Spectroscopic Studies of [L2Fe2S2] n Model Complexes: Implications for the Experimental Evaluation of Redox States in Iron–Sulfur Clusters
Kowalska, J. K., Hahn, A. W., Albers, A., Schiewer, C. E., Björnsson, R., Lima, F. A., Meyer, F., & DeBeer, S. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b00295 · Cited by 90
Interplay of IscA and IscU in Biogenesis of Iron-Sulfur Clusters
Yang, J., Bitoun, J. P., & Ding, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601356200 · Cited by 89
Biogenesis of Iron–Sulfur Clusters and Their Role in DNA Metabolism
Shi, R., Hou, W., Wang, Z., & Xu, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.735678 · Cited by 91
Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly
Schwenkert, S., Netz, D. J. A., Frazzon, J., Pierik, A. J., Bill, E., Gross, J., Lill, R., & Meurer, J. (2009) · Biochemical Journal · doi:10.1042/bj20091290 · Cited by 92
Characterization of Arabidopsis thaliana SufE2 and SufE3
Narayana Murthy, U. M., de Choudens, S. O., Sanakis, Y., Abdel‐Ghany, S. E., Rousset, C., Ye, H., Fontecave, M., Pilon‐Smits, E. A. H., & Pilon, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701428200 · Cited by 88
Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria
Molina‐Navarro, M. M., Casas, C., Piedrafita, L., Bellı́, G., & Herrero, E. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.037 · Cited by 87
Highly Covalent Ferric−Thiolate Bonds Exhibit Surprisingly Low Mechanical Stability
Zheng, P., & Li, H. (2011) · Journal of the American Chemical Society · doi:10.1021/ja200715h · Cited by 89
Facilitated Transfer of IscU–[2Fe2S] Clusters by Chaperone-Mediated Ligand Exchange
Bonomi, F., Iametti, S., Morleo, A., Ta, D. T., & Vickery, L. E. (2011) · Biochemistry · doi:10.1021/bi201123z · Cited by 87
Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv
Alam†, M. S., Garg†, S. K., & Agrawal, P. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06755.x · Cited by 86
AirSR, a [2Fe-2S] Cluster-Containing Two-Component System, Mediates Global Oxygen Sensing and Redox Signaling in Staphylococcus aureus
Sun, F., Ji, Q., Jones, M. B., Deng, X., Liang, H., Frank, B. C., Telser, J., Peterson, S. N., Bae, T., & He, C. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2071835 · Cited by 85
Arabidopsis thaliana Nfu2 Accommodates [2Fe-2S] or [4Fe-4S] Clusters and Is Competent for in Vitro Maturation of Chloroplast [2Fe-2S] and [4Fe-4S] Cluster-Containing Proteins
Gao, H., Sowmya, S., Couturier, J., Naik, S., Kim, S., Leustek, T., Knaff, D. B., Wu, H.-C., Vignols, F., Huynh, B. H., et al. (2013) · Biochemistry · doi:10.1021/bi4007622 · Cited by 84
“IscU was shown to be the primary Fe-S cluster scaffold associated with the ISC machinery for Fe-S cluster assembly that is responsible for cluster assembly in most bacteria and in eukaryotic mitochondria (2;6).”
Background
Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron–sulfur cluster biosynthesis and delivery
Markley, J. L., Kim, J. H., Dai, Z., Bothe, J. R., Cai, K., Frederick, R. O., & Tonelli, M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.003 · Cited by 88
“Cells have evolved elaborate mechanisms for producing iron–sulfur clusters so as to minimize exposure to their toxic constituents, iron and sulfur ions [2,3].”
Background
Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase
Kim, J. H., Tonelli, M., & Markley, J. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114372109 · Cited by 84
“The bacterial system utilizes several proteins that have eukaryotic homologs: IscU (scaffold protein), IscS (cysteine desulfurase), HscB (cochaperone), HscA (chaperone), and CyaY (regulation or iron delivery, analog of human frataxin) (1).”
Background
A review on application of single and composite conductive additives for anaerobic digestion: Advances, challenges and prospects
Liu, H., Xu, Y., Li, L., Dai, X., & Dai, L. (2021) · Resources Conservation and Recycling · doi:10.1016/j.resconrec.2021.105844 · Cited by 85
Fe-S Cluster Biogenesis in Gram-Positive Bacteria: SufU Is a Zinc-Dependent Sulfur Transfer Protein
Selbach, B. P., Chung, A. H., Scott, A. D., George, S. J., Cramer, S. P., & Santos, P. C. D. (2013) · Biochemistry · doi:10.1021/bi4011978 · Cited by 83
Emerging Paradigms for Complex Iron-Sulfur Cofactor Assembly and Insertion
Peters, J. W., & Broderick, J. B. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052610-094911 · Cited by 84
A Trapping Approach Reveals Novel Substrates and Physiological Functions of the Essential Protease FtsH in Escherichia coli
Westphal, K., Schäkermann, S., Thomanek, N., & Narberhaus, F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.388470 · Cited by 82
“It is a cysteine desulfurase responsible for iron-sulfur cluster formation and sulfatation of thiamine and biotin (46).”
Background
A radical solution for the biosynthesis of the H‐cluster of hydrogenase
Peters, J. W., Szilagyi, R. K., Naumov, A. V., & Douglas, T. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.12.040 · Cited by 82
“metal cluster assembly on a scaffold and subsequent insertion into a target protein has been experimentally established for both the general synthesis of [4Fe–4S] clusters in proteins [22] and for the biosynthesis and insertion of the FeMo-cofactor for the enzyme nitrogenase [23].”
Background
Catalysis and Electron Transfer in De Novo Designed Metalloproteins
Koebke, K. J., Pinter, T. B. J., Pitts, W. C., & Pecoraro, V. L. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01025 · Cited by 84
Production of ethylene glycol or glycolic acid from D-xylose in Saccharomyces cerevisiae
Salusjärvi, L., Toivari, M. H., Vehkomäki, M., Koivistoinen, O. M., Mojžita, D., Niemelä, K., Penttilä, M. E., & Ruohonen, L. (2017) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-017-8547-3 · Cited by 81
Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication
Barton, J. K., Silva, R. M. B., & O’Brien, E. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110644 · Cited by 77
“However each process requires the concerted action of several specialized proteins and requires significant metabolic expense for the cell (13-19).”
Background
Nitric oxide‐induced bacteriostasis and modification of iron‐sulphur proteins in Escherichia coli
Ren, B., Zhang, N., Yang, J., & Ding, H. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06464.x · Cited by 80
“Iron-sulphur proteins are involved in diverse physiological processes with over 200 unique iron-sulphur proteins identified so far (Johnson et al., 2005; Lill and Muhlenhoff, 2006).”
Background
The indispensable role of mammalian iron sulfur proteins in function and regulation of multiple diverse metabolic pathways
Rouault, T. A. (2019) · BioMetals · doi:10.1007/s10534-019-00191-7 · Cited by 84
Hydrosulfide complexes of the transition elements: diverse roles in bioinorganic, cluster, coordination, and organometallic chemistry
Pluth, M. D., & Tonzetich, Z. J. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00570f · Cited by 82
A Novel DNA Modification by Sulfur: DndA Is a NifS-like Cysteine Desulfurase Capable of Assembling DndC as an Iron−Sulfur Cluster Protein in Streptomyces lividans
You, D., Wang, L., Yao, F., Zhou, X., & Deng, Z. (2007) · Biochemistry · doi:10.1021/bi602615k · Cited by 79
Simultaneous Enrichment of Cysteine-containing Peptides and Phosphopeptides Using a Cysteine-specific Phosphonate Adaptable Tag (CysPAT) in Combination with titanium dioxide (TiO2) Chromatography
Huang, H., Petersen, M. H., Ibáñez-Vea, M., Lassen, P. S., Larsen, M. R., & Palmisano, G. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054551 · Cited by 74
Accumulation of 2‐C‐methyl‐ d ‐erythritol 2,4‐cyclodiphosphate in illuminated plant leaves at supraoptimal temperatures reveals a bottleneck of the prokaryotic methylerythritol 4‐phosphate pathway of isoprenoid biosynthesis
Rivasseau, C., Seemann, M., Boisson, A., Streb, P., Gout, E., Douce, R., Rohmer, M., & Bligny, R. (2008) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2008.01903.x · Cited by 78
The self-organizing fractal theory as a universal discovery method: the phenomenon of life
Kurakin, A. V. (2011) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-8-4 · Cited by 84
“The ability to delocalize electron density over both Fe and S atoms makes [Fe-S] clusters ideally suited for mediating electron transport [91,92].”
Background
A genetic analysis of the response of Escherichia coli to cobalt stress
Fantino, J., Py, B., Fontecave, M., & Barras, F. (2010) · Environmental Microbiology · doi:10.1111/j.1462-2920.2010.02265.x · Cited by 77
A π-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase
Medlock, A. E., Dailey, T. A., Ross, T. A., Dailey, H. A., & Lanzilotta, W. N. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.08.040 · Cited by 77
Binding of Histidine in the (Cys)3(His)1-Coordinated [2Fe−2S] Cluster of Human mitoNEET
Dicus, M. M., Conlan, A. R., Nechushtai, R., Jennings, P. A., Paddock, M. L., Britt, R. D., & Stoll, S. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909359g · Cited by 77
Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli
Fontenot, C. R., Tasnim, H., Valdes, K. A., Popescu, C. V., & Ding, H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014814 · Cited by 74
A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis
Song, D., & Lee, F. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708077200 · Cited by 79
Reprint of: Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity
Roche, B., Aussel, L., Ezraty, B., Mandin, P., Py, B., & Barras, F. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.05.001 · Cited by 80
Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe–S Assembly Complex
Fox, N. G., Das, D., Chakrabarti, M., Lindahl, P. A., & Barondeau, D. P. (2015) · Biochemistry · doi:10.1021/bi5014497 · Cited by 76
From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis
Lill, R. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0117 · Cited by 73
The Sulfur Carrier Protein TusA Has a Pleiotropic Role in Escherichia coli That Also Affects Molybdenum Cofactor Biosynthesis*
Dahl, J., Radon, C., Bühning, M., Nimtz, M., Leichert, L. I. O., Denis, Y., Jourlin‐Castelli, C., Iobbi‐Nivol, C., Méjean, V., & Leimkühler, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431569 · Cited by 75
“In Escherichia coli, the iron-sulfur cluster (ISC)(2) system fulfills a housekeeping function (3).”
Background
Molecular view of an electron transfer process essential for iron–sulfur protein biogenesis
Banci, L., Bertini, I., Calderone, V., Ciofi‐Baffoni, S., Giachetti, A., Jaiswal, D., Mikołajczyk, M., Piccioli, M., & Winkelmann, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302378110 · Cited by 75
“Prog Nucl Magn Reson Spectrosc 48(1):25–45.”
Molecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: a [4Fe−4S] cluster co‐ordinating protein disulphide reductase
Alam†, M. S., Garg†, S. K., & Agrawal, P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05589.x · Cited by 76
“Iron–sulphur clusters are nature’s most fascinating, ubiquitous, evolutionary ancient and are among the most structurally and functionally versatile cofactors in biology (Beinert et al., 1997; Johnson et al., 2005).”
Background
Iron–sulfur clusters biogenesis by the SUF machinery: close to the molecular mechanism understanding
Pérard, J., & de Choudens, S. O. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1527-3 · Cited by 83
Biosynthesis of nitrogenase FeMoco
Hu, Y., & Ribbe, M. W. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.11.018 · Cited by 74
The Impact of O2 on the Fe–S Cluster Biogenesis Requirements of Escherichia coli FNR
Mettert, E. L., Outten, F. W., Wanta, B. T., & Kiley, P. J. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.080 · Cited by 73
Role of IscX in Iron–Sulfur Cluster Biogenesis in Escherichia coli
Kim, J. H., Bothe, J. R., Frederick, R. O., Holder, J. C., & Markley, J. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja501260h · Cited by 73
Reactivity of nitric oxide with the [4Fe–4S] cluster of dihydroxyacid dehydratase fromEscherichia coli
Duan, X., Yang, J., Ren, B., Tan, G., & Ding, H. (2008) · Biochemical Journal · doi:10.1042/bj20081423 · Cited by 74
Heavy chalcogenide-transition metal clusters as coordination polymer nodes
Xie, J., Wang, L., & Anderson, J. S. (2020) · Chemical Science · doi:10.1039/d0sc03429k · Cited by 75
Structure–Function Analysis of Friedreich’s Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe–S Assembly Complex
Bridwell‐Rabb, J., Winn, A. M., & Barondeau, D. P. (2011) · Biochemistry · doi:10.1021/bi200895k · Cited by 72
Transcriptional response of Burkholderia cenocepacia J2315 sessile cells to treatments with high doses of hydrogen peroxide and sodium hypochlorite
Peeters, E., Sass, A. M., Mahenthiralingam, E., Nelis, H. J. C. F., & Coenye, T. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-90 · Cited by 75
“coli, apo-IscR will increase the transcription of the isc gene cluster, and together with OxyR it will also stimulate the production of oxidation-resistant Suf proteins [46].”
Iron–sulfur clusters: from metals through mitochondria biogenesis to disease
Cardenas‐Rodriguez, M., Chatzi, A., & Tokatlidis, K. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1548-6 · Cited by 76
“In addition, loss of one Fe ions of that form leads to the non-symmetrical [3Fe–4S] structure [10].”
Background
Engineering Nitrogenases for Synthetic Nitrogen Fixation: From Pathway Engineering to Directed Evolution
Bennett, E. M., Murray, J. W., & Isalan, M. (2023) · BioDesign Research · doi:10.34133/bdr.0005 · Cited by 79
Fe 2+ binds iron responsive element-RNA, selectively changing protein-binding affinities and regulating mRNA repression and activation
Ma, J., Haldar, S., Khan, M. A., Sharma, S. D., Merrick, W. C., Theil, E. C., & Goss, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120045109 · Cited by 72
Monothiol glutaredoxin Grx5 interacts with Fe–S scaffold proteins Isa1 and Isa2 and supports Fe–S assembly and DNA integrity in mitochondria of fission yeast
Kim, K.-D., Chung, W., Kim, H.-J., Lee, K.-C., & Roe, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.051 · Cited by 71
Coordinate Regulation of the Suf and Isc Fe-S Cluster Biogenesis Pathways by IscR Is Essential for Viability of Escherichia coli
Mettert, E. L., & Kiley, P. J. (2014) · Journal of Bacteriology · doi:10.1128/jb.01975-14 · Cited by 71
Using synthetic biology to increase nitrogenase activity
Li, X., Liu, Q., Liu, X., Shi, H., & Chen, S. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0442-6 · Cited by 71
“coli has two ironsulfur cluster assembly systems: the sufABCDSE operon and the isc system composed of iscR, iscS, iscU, iscA, hscB, hscA, fdx, and orf3 [17].”
Background
Anaerobic Copper Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli
Tan, G., Yang, J., Li, T., Jin, Z., Sun, S., Li, X., Lin, C., Li, J., Zhou, H., Lyu, J., et al. (2017) · Applied and Environmental Microbiology · doi:10.1128/aem.00867-17 · Cited by 76
“Since iron-sulfur proteins are involved in diverse and vital physiological processes (17, 18), inactivation of iron-sulfur cluster biogenesis by copper would have a broad effect on cellular functions under anaerobic conditions.”
Background
X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe 4 S 4 clusters
Nicolet, Y., Rohac, R., Martin, L., & Fontecilla-Camps, J. C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302388110 · Cited by 70
“They can be involved in electron transfer, substrate binding and activation, be used as stress sensors to regulate gene expression or simply play a structural role (1).”
Background

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

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

STRUCTURE, FUNCTION, AND FORMATION OF BIOLOGICAL IRON-SULFUR CLUSTERS

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks