Structure, function, and formation of biological iron-sulfur clusters

Johnson, Deborah C.; Dean, Dennis R.; Smith, Archer D.; Johnson, Michael K.

doi:10.1146/annurev.biochem.74.082803.133518

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

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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Fe-S clusters are ubiquitous inorganic co-factors that contribute to genome integrity, gene regulation, energy production, and immune responses, and are required for numerous biological functions, particularly enzymatic activity.
“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
Iron acts alone or in iron-sulfur clusters as a prosthetic moiety for oxidoreductase, nitrogenase, hydrogenase, dehydrogenase, and hydratase enzyme families.
“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]

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 · see citing works
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 · see citing works
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8&nbsp;Angstrom Resolution
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606 · see citing works
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
Zheng, L., White, R. H., Cash, V. L., Jack, R. F., & Dean, D. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2754 · Cited by 597 · see citing works
Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster
Dobbek, H., Svetlitchnyi, V. A., Gremer, L., Huber, R., & Meyer, O. O. (2001) · Science · doi:10.1126/science.1061500 · Cited by 570 · see citing works
A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase
Doukov, T. I., Iverson, T. M., Seravalli, J., Ragsdale, S. W., & Drennan, C. L. (2002) · Science · doi:10.1126/science.1075843 · Cited by 529 · see citing works
Redox-Dependent Structural Changes in the Nitrogenase P-Cluster,
Peters, J. W., Stowell, M. H. B., Stowell, M. H. B., Finnegan, M. G., Johnson, M. K., & Rees, D. C. (1997) · Biochemistry · doi:10.1021/bi9626665 · Cited by 481 · see citing works
Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0517 · Cited by 464 · see citing works
A Third Bacterial System for the Assembly of Iron-Sulfur Clusters with Homologs in Archaea and Plastids
Takahashi, Y., & Tokumoto, U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200365200 · Cited by 456 · see citing works
A suf operon requirement for Fe–S cluster assembly during iron starvation in Escherichia coli
Outten, F. W., Djaman, O., & Storz, G. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04025.x · Cited by 448 · see citing works
IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
Schwartz, C. J., Giel, J. L., Patschkowski, T., Luther, C., Ruzicka, F. J., Beinert, H., & Kiley, P. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251550898 · Cited by 442 · see citing works
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
Darnault, C., Volbeda, A., Kim, E., Legrand, P., Vernède, X., Lindahl, P. A., & Fontecilla-Camps, J. C. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb912 · Cited by 432 · see citing works
IscU as a Scaffold for Iron−Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscU
Agar, J. N., Krebs, C., Jeverson Frazzon, B., Huynh, B. H., Dean, D. R., & Johnson, M. K. (2000) · Biochemistry · doi:10.1021/bi000931n · Cited by 430 · see citing works
Crystal Structure of Biotin Synthase, an S -Adenosylmethionine-Dependent Radical Enzyme
Berkovitch, F., Nicolet, Y., Wan, J. T., Jarrett, J. T., & Drennan, C. L. (2004) · Science · doi:10.1126/science.1088493 · Cited by 424 · see citing works
Mechanism for the Desulfurization of L-Cysteine Catalyzed by the nifS Gene Product
Zheng, L., White, R. H., Cash, V. L., & Dean, D. R. (1994) · Biochemistry · doi:10.1021/bi00181a031 · Cited by 395 · see citing works
Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p
Mühlenhoff, U., Gerber, J., Richhardt, N., & Lill, R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg446 · Cited by 383 · see citing works
Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii
Jacobson, M. R., Brigle, K. E., Bennett, L. T., Setterquist, R. A., Wilson, M. S., Cash, V. L., Beynon, J., Newton, W. E., & Dean, D. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.1017-1027.1989 · Cited by 373 · see citing works
The role of Fe–S proteins in sensing and regulation in bacteria
Kiley, P. J., & Beinert, H. (2003) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(03)00039-0 · Cited by 363 · see citing works
Iron−Sulfur Cluster Biosynthesis. Characterization of Frataxin as an Iron Donor for Assembly of [2Fe-2S] Clusters in ISU-Type Proteins
Yoon, T., & Cowan, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja027967i · Cited by 353 · see citing works
Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions
Crane, B. R., Siegel, L. M., & Getzoff, E. D. (1995) · Science · doi:10.1126/science.270.5233.59 · Cited by 345 · see citing works
An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
Gerber, J., Mühlenhoff, U., & Lill, R. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor918 · Cited by 334 · see citing works
NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein
Yuvaniyama, P., Agar, J. N., Cash, V. L., Johnson, M. K., & Dean, D. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.599 · Cited by 330 · see citing works
Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii
Jacobson, M. R., Cash, V. L., Weiss, M. C., Laird, N. F., Newton, W. E., & Dean, D. R. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00261156 · Cited by 329 · see citing works
Ligand K-Edge X-ray Absorption Spectroscopy: A Direct Probe of Ligand−Metal Covalency
Glaser, T., Hedman, B., Hodgson, K. O., & Solomon, E. I. (2000) · Accounts of Chemical Research · doi:10.1021/ar990125c · Cited by 329 · see citing works
MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily
Guan, Y., Manuel, R. C., Arvai, A. S., Parikh, S. S., Mol, C. D., Miller, J. H., Lloyd, R. S., & Tainer, J. A. (1998) · Nature Structural Biology · doi:10.1038/4168 · Cited by 325 · see citing works
Bacterial cysteine desulfurases: their function and mechanisms
Mihara, H., & Esaki, N. (2002) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-002-1107-4 · Cited by 310 · see citing works
The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli
Outten, F. W., Wood, M. J. A., Muñoz, F. M., & Storz, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308004200 · Cited by 302 · see citing works
The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
Schwartz, C. J., Djaman, O., Imlay, J. A., & Kiley, P. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160261497 · Cited by 301 · see citing works
Nitrogenase: standing at the crossroads
Rees, D. C., & Howard, J. B. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00132-0 · Cited by 300 · see citing works
Atomic Structure of the DNA Repair [4Fe-4S] Enzyme Endonuclease III
Kuo, C.-F., McRee, D. E., Fisher, C. L., O’Handley, S., Cunningham, R. P., & Tainer, J. A. (1992) · Science · doi:10.1126/science.1411536 · Cited by 289 · see citing works
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
Schilke, B. A., Voisine, C., Beinert, H., & Craig, E. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10206 · Cited by 284 · see citing works
Iron–sulfur proteins with nonredox functions
Flint, D. H., & Allen, R. M. (1996) · Chemical Reviews · doi:10.1021/cr950041r · Cited by 280 · see citing works
SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe—S] biogenesis under oxidative stress
Nachin, L., Loiseau, L., Expert, D., & Barras, F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg061 · Cited by 278 · see citing works
Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly
Urbina, H. D., Silberg, J. J., Hoff, K. G., & Vickery, L. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106907200 · Cited by 278 · see citing works
A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
Lange, H., Kaut, A., Kispál, G., & Lill, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1050 · Cited by 272 · see citing works
A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans
Svetlitchnyi, V. A., Dobbek, H., Meyer‐Klaucke, W., Meins, T., Thiele, B., Römer, P., Huber, R., & Meyer, O. O. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0304262101 · Cited by 260 · see citing works
Genetic Analysis of the isc Operon in Escherichia coli Involved in the Biogenesis of Cellular Iron-Sulfur Proteins
Tokumoto, U., & Takahashi, Y. (2001) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a002963 · Cited by 254 · see citing works
IscA, an Alternate Scaffold for Fe−S Cluster Biosynthesis
Krebs, C., Agar, J. N., Smith, A. D., Jeverson Frazzon, B., Dean, D. R., Huynh, B. H., & Johnson, M. K. (2001) · Biochemistry · doi:10.1021/bi015656z · Cited by 252 · see citing works
Functional Assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-0RF3 Gene Cluster Involved in the Assembly of Fe-S Clusters in Escherichia coli
Takahashi, Y., & Nakamura, M. (1999) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022535 · Cited by 247 · see citing works
Structure of the Allosteric Regulatory Enzyme of Purine Biosynthesis
Smith, J. L., Zaluzec, E. J., Wery, J., Niu, L., Switzer, R. L., Zalkin, H., & Satow, Y. (1994) · Science · doi:10.1126/science.8197456 · Cited by 242 · see citing works
Fe-only hydrogenases: structure, function and evolution
Nicolet, Y., Cavazza, C., & Fontecilla-Camps, J. C. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00392-6 · Cited by 236 · see citing works
Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.
Brehmer, D., Rüdiger, S., Gässler, C. S., Klostermeier, D., Packschies, L., Reinstein, J., Mayer, M. P., & Bukau, B. (2001) · Nature Structural Biology · doi:10.1038/87588 · Cited by 231 · see citing works
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
(2001) · Nature Structural Biology · doi:10.1038/84152 · Cited by 227 · see citing works
Biogenesis of Fe-S Cluster by the Bacterial Suf System
Loiseau, L., de Choudens, S. O., Nachin, L., Fontecave, M., & Barras, F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305953200 · Cited by 226 · see citing works
Interaction of the iron–sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
Hoff, K. G., Silberg, J. J., & Vickery, L. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130201997 · Cited by 222 · see citing works
Endonuclease III is an iron-sulfur protein
Cunningham, R. P., Asahara, H., Bank, J. F., Scholes, C. P., Salerno, J. C., Surerus, K. K., Münck, E., McCracken, J., Peisach, J., & Emptage, M. H. (1989) · Biochemistry · doi:10.1021/bi00436a049 · Cited by 221 · see citing works
The reconstitution of clostridial ferredoxin
Malkin, R., & Rabinowitz, J. C. (1966) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(66)90561-4 · Cited by 213 · see citing works
Iron-Sulfur Cluster Assembly
de Choudens, S. O., Mattioli, T. A., Takahashi, Y., & Fontecave, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102902200 · Cited by 211 · see citing works
Catalytic formation of a nitrogenase iron-sulfur cluster.
Zheng, L., & Dean, D. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32225-1 · Cited by 207 · see citing works
The hydrogenase‐like Nar1p is essential for maturation of cytosolic and nuclear iron–sulphur proteins
Balk, J., Pierik, A. J., Netz, D. J. A., Mühlenhoff, U., & Lill, R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600216 · Cited by 206 · see citing works
Biogenesis of iron–sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria
Mühlenhoff, U., & Lill, R. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00174-2 · Cited by 204 · see citing works
Hyperproduction of Recombinant Ferredoxins in Escherichia coli by Coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 Gene Cluster
Nakamura, M., Saeki, K., & Takahashi, Y. (1999) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022409 · Cited by 203 · see citing works
Redox Signaling in Chloroplasts: Cleavage of Disulfides by an Iron-Sulfur Cluster
Dai, S., Schwendtmayer, C., Schürmann, P., Ramaswamy, S., & Eklund, H. (2000) · Science · doi:10.1126/science.287.5453.655 · Cited by 200 · see citing works
The iscS Gene in Escherichia coli Is Required for the Biosynthesis of 4-Thiouridine, Thiamin, and NAD
Lauhon, C. T., & Kambampati, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002680200 · Cited by 199 · see citing works
Sulfur Transfer from IscS to IscU: The First Step in Iron−Sulfur Cluster Biosynthesis
Smith, A. D., Agar, J. N., Johnson, K. A., Jeverson Frazzon, B., Amster, I. J., Dean, D. R., & Johnson, M. K. (2001) · Journal of the American Chemical Society · doi:10.1021/ja016757n · Cited by 194 · see citing works
Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
Tong, W.-H., Jameson, G. N. L., Huynh, B. H., & Rouault, T. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1732541100 · Cited by 194 · see citing works
Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly
Garland, S. A., Hoff, K. G., Vickery, L. E., & Culotta, V. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3294 · Cited by 192 · see citing works
Crystal Structure of IscS, a Cysteine Desulfurase from Escherichia coli
Cupp‐Vickery, J. R., Urbina, H. D., & Vickery, L. E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00690-9 · Cited by 187 · see citing works
Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae
Strain, J., Lorenz, C. R., Bode, J., Garland, S., Smolen, G. A., Ta, D. T., Vickery, L. E., & Culotta, V. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31138 · Cited by 181 · see citing works
SoxR‐dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase
Nachin, L., Hassouni, M. E., Loiseau, L., Expert, D., & Barras, F. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02288.x · Cited by 180 · see citing works
Mitochondrial Type Iron-Sulfur Cluster Assembly in the Amitochondriate Eukaryotes Trichomonas vaginalis and Giardia intestinalis, as Indicated by the Phylogeny of IscS
Tachezy, J., Sánchez, L. B., & Müller, M. (2001) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a003732 · Cited by 180 · see citing works
Mt-Hsp70 Homolog, Ssc2p, Required for Maturation of Yeast Frataxin and Mitochondrial Iron Homeostasis
Knight, S. A. B., Sepuri, N. B. V., Pain, D., & Dancis, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18389 · Cited by 173 · see citing works
Role of Saccharomyces cerevisiae ISA1 and ISA2 in Iron Homeostasis
Jensen, L. T., & Culotta, V. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.11.3918-3927.2000 · Cited by 173 · see citing works
MnmA and IscS Are Required for in Vitro 2-Thiouridine Biosynthesis in Escherichia coli
Kambampati, R., & Lauhon, C. T. (2003) · Biochemistry · doi:10.1021/bi026536+ · Cited by 168 · see citing works
Evidence That ThiI, an Enzyme Shared between Thiamin and 4-Thiouridine Biosynthesis, May Be a Sulfurtransferase That Proceeds through a Persulfide Intermediate
Palenchar, P. M., Buck, C. J., Cheng, H. W., Larson, T. J., & Mueller, E. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8283 · Cited by 168 · see citing works
Cysteine Sulfinate Desulfinase, a NIFS-like Protein ofEscherichia coli with Selenocysteine Lyase and Cysteine Desulfurase Activities
Mihara, H., Kurihara, T., Yoshimura, T., Soda, K., & Esaki, N. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22417 · Cited by 165 · see citing works
Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role
Cheek, J., & Broderick, J. B. (2001) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750100210 · Cited by 162 · see citing works
Induction of the sufA operon encoding Fe‐S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant‐responsive factor
Lee, J. L., Yeo, W., & Roe, J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2003.03946.x · Cited by 161 · see citing works
A novel eukaryotic factor for cytosolic Fe–S cluster assembly
Roy, A., Solodovnikova, N., Nicholson, T., Antholine, W. E., & Walden, W. E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg455 · Cited by 160 · see citing works
Bacillus subtilis aconitase is an RNA-binding protein
Amaro, C. A., & Sonenshein, A. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10412 · Cited by 159 · see citing works
Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
Tang, Y., & Guest, J. R. (1999) · Microbiology · doi:10.1099/00221287-145-11-3069 · Cited by 158 · see citing works
The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
Huynen, M. A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.21.2463 · Cited by 157 · see citing works
SufS Is a NifS-Like Protein, and SufD Is Necessary for Stability of the [2Fe-2S] FhuF Protein in Escherichia coli
Patzer, S. I., & Hantke, K. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.10.3307-3309.1999 · Cited by 155 · see citing works
Kinetic and Mutational Studies of Three NifS Homologs from Escherichia coli: Mechanistic Difference between L-Cysteine Desulfurase and L-Selenocysteine Lyase Reactions
Mihara, H., Kurihara, T., Yoshimura, T., & Esaki, N. (2000) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022641 · Cited by 152 · see citing works
Evidence for the Transfer of Sulfane Sulfur from IscS to ThiI during the in Vitro Biosynthesis of 4-Thiouridine inEscherichia coli tRNA
Kambampati, R., & Lauhon, C. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10727 · Cited by 151 · see citing works
Iron-Sulfur Cluster Assembly
Santos, P. C. D., Smith, A. D., Jeverson Frazzon, B., Cash, V. L., Johnson, M. K., & Dean, D. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400278200 · Cited by 150 · see citing works
nifU Gene Product from Azotobacter vinelandii Is a Homodimer That Contains Two Identical [2Fe-2S] Clusters
Fu, W., Jack, R. F., Morgan, T., Dean, D. R., & Johnson, M. K. (1994) · Biochemistry · doi:10.1021/bi00249a034 · Cited by 149 · see citing works
Definition of reaction sequences resulting in self-assembly of [Fe4S4(SR)4]2- clusters from simple reactants
Hagen, K. S., Reynolds, J. G., & Holm, R. H. (1981) · Journal of the American Chemical Society · doi:10.1021/ja00404a013 · Cited by 149 · see citing works
Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis
Šuťák, R., Doležal, P., Fiumera, H. L., Hrdý, I., Dancis, A., Delgadillo‐Correa, M. G., Johnson, P. J., Müller, M., & Tachezy, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401319101 · Cited by 147 · see citing works
Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly
Kaiser, J. T., Clausen, T., Bourenkow, G., Bartunik, H. D., Steinbacher, S., & Huber, R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3581 · Cited by 146 · see citing works
Nucleotide sequence and mutational analysis of the structural genes (anfHDGK) for the second alternative nitrogenase from Azotobacter vinelandii
Joerger, R. D., Jacobson, M. R., Premakumar, R., Wolfinger, E. D., & Bishop, P. E. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.1075-1086.1989 · Cited by 143 · see citing works
Biotin Synthase Contains Two Distinct Iron−Sulfur Cluster Binding Sites: Chemical and Spectroelectrochemical Analysis of Iron−Sulfur Cluster Interconversions
Ugulava, N. B., Gibney, B. R., & Jarrett, J. T. (2001) · Biochemistry · doi:10.1021/bi0104625 · Cited by 142 · see citing works
Function of the [2Fe−2S] Cluster in Mammalian Ferrochelatase: A Possible Role as a Nitric Oxide Sensor
Sellers, V. M., Johnson, M. K., & Dailey, H. A. (1996) · Biochemistry · doi:10.1021/bi952631p · Cited by 139 · see citing works
Biosynthesis of the Thiazole Moiety of Thiamin Pyrophosphate (Vitamin B1)
Park, J.-H., Dorrestein, P. C., Zhai, H., Kinsland, C. L., McLafferty, F. W., & Begley, T. P. (2003) · Biochemistry · doi:10.1021/bi034902z · Cited by 133 · see citing works
Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae
Voisine, C., Cheng, Y. C., Ohlson, M. B., Schilke, B. A., Hoff, K. G., Beinert, H., Marszałek, J., & Craig, E. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1483 · Cited by 131 · see citing works
The Role of the Cysteine Residues of ThiI in the Generation of 4-Thiouridine in tRNA
Mueller, E. G., Palenchar, P. M., & Buck, C. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104067200 · Cited by 130 · see citing works
Iron Binding and Oxidation Kinetics in Frataxin CyaY of Escherichia coli
Bou‐Abdallah, F., Adinolfi, S., Pastore, A., Laue, T. M., & Chasteen, N. D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.072 · Cited by 129 · see citing works
Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein
Ding, H., & CLARK, R. J. (2004) · Biochemical Journal · doi:10.1042/bj20031702 · Cited by 129 · see citing works
Ssq1, a Mitochondrial Hsp70 Involved in Iron-Sulfur (Fe/S) Center Biogenesis
Dutkiewicz, R., Schilke, B. A., Knieszner, H., Walter, W. A., Craig, E. A., & Marszałek, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303527200 · Cited by 128 · see citing works
Modular organization and identification of a mononuclear iron-binding site within the NifU protein
Agar, J. N., Yuvaniyama, P., Jack, R. F., Cash, V. L., Smith, A. D., Dean, D. R., & Johnson, M. K. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050361 · Cited by 128 · see citing works
Chaperone-Assisted Protein Folding in the Cell Cytoplasm
Houry, W. A. (2001) · Current Protein and Peptide Science · doi:10.2174/1389203013381134 · Cited by 127 · see citing works
The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
Lutz, T., Westermann, B., Neupert, W., & Herrmann, J. M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4527 · Cited by 125 · see citing works
A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain delta H encodes a polyferredoxin.
Reeve, J. N., Beckler, G. S., Cram, D. S., Hamilton, P. T., Brown, J. W., Krzycki, J. A., Kolodziej, A. F., Alex, L. A., Orme-Johnson, W. H., & Walsh, C. T. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3031 · Cited by 125 · see citing works
Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly
Kato, S.-I., Mihara, H., Kurihara, T., Takahashi, Y., Tokumoto, U., Yoshimura, T., & Esaki, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082123599 · Cited by 124 · see citing works
Identification of a gene involved in the generation of 4-thiouridine in tRNA
Mueller, E. G. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.11.2606 · Cited by 124 · see citing works
Characterization of Iron-Sulfur Protein Assembly in Isolated Mitochondria
Mühlenhoff, U., Richhardt, N., Gerber, J., & Lill, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204675200 · Cited by 122 · see citing works
Isa1p Is a Component of the Mitochondrial Machinery for Maturation of Cellular Iron-Sulfur Proteins and Requires Conserved Cysteine Residues for Function
Kaut, A., Lange, H., Diekert, K., Kispál, G., & Lill, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909502199 · Cited by 122 · see citing works
Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock
Lelivelt, M. J., & Kawula, T. H. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.17.4900-4907.1995 · Cited by 121 · see citing works
A nifS-like Gene, csdB, Encodes anEscherichia coli Counterpart of Mammalian Selenocysteine Lyase
Mihara, H., Maeda, M., Fujii, T., Kurihara, T., Hata, Y., & Esaki, N. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14768 · Cited by 120 · see citing works
IscS Is a Sulfurtransferase for the in Vitro Biosynthesis of 4-Thiouridine in Escherichia coli tRNA
Kambampati, R., & Lauhon, C. T. (1999) · Biochemistry · doi:10.1021/bi991119r · Cited by 118 · see citing works
An Intestinal Parasitic Protist, Entamoeba histolytica, Possesses a Non-redundant Nitrogen Fixation-like System for Iron-Sulfur Cluster Assembly under Anaerobic Conditions
Ali, V., Shigeta, Y., Tokumoto, U., Takahashi, Y., & Nozaki, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313314200 · Cited by 117 · see citing works
Requirement for IscS in Biosynthesis of All Thionucleosides in Escherichia coli
Lauhon, C. T. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.24.6820-6829.2002 · Cited by 116 · see citing works
Mitochondrial functional interactions between frataxin and Isu1p, the iron–sulfur cluster scaffold protein, in Saccharomyces cerevisiae
Ramazzotti, A., Vanmansart, V., & Foury, F. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01498-4 · Cited by 116 · see citing works
The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins
Gerber, J., Neumann, K., Prohl, C., Mühlenhoff, U., & Lill, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4848-4857.2004 · Cited by 115 · see citing works
Identification of the miaB Gene, Involved in Methylthiolation of Isopentenylated A37 Derivatives in the tRNA of Salmonella typhimurium and Escherichia coli
Esberg, B., Leung, H. E., Tsui, H. T., Björk, G. R., & Winkler, M. E. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.23.7256-7265.1999 · Cited by 114 · see citing works
Iron-sulphur cluster assembly in plants: distinct NFU proteins in mitochondria and plastids from Arabidopsis thaliana
Sébastien Léon, A., Touraine, B., Ribot, C., Briat, J., & LOBÉRAUX, S. (2003) · Biochemical Journal · doi:10.1042/bj20021946 · Cited by 112 · see citing works
Transfer of Iron-Sulfur Cluster from NifU to Apoferredoxin
Nishio, K., & Nakai, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000279200 · Cited by 112 · see citing works
Role of the IscU Protein in Iron−Sulfur Cluster Biosynthesis: IscS-mediated Assembly of a [Fe2S2] Cluster in IscU
Agar, J. N., Zheng, L., Cash, V. L., Dean, D. R., & Johnson, M. K. (2000) · Journal of the American Chemical Society · doi:10.1021/ja9944195 · Cited by 110 · see citing works
Enzymatic Modification of tRNAs
Pierrel, F., Björk, G. R., Fontecave, M., & Atta, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100609200 · Cited by 110 · see citing works
Hsc66 Substrate Specificity Is Directed toward a Discrete Region of the Iron-Sulfur Cluster Template Protein IscU
Hoff, K. G., Ta, D. T., Tapley, T. L., Silberg, J. J., & Vickery, L. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202814200 · Cited by 110 · see citing works
A Substrate Recognition Role for the [4Fe-4S]2+ Cluster of the DNA Repair Glycosylase MutY
Porello, S. L., Cannon, M. J., & David, S. S. (1998) · Biochemistry · doi:10.1021/bi972433t · Cited by 108 · see citing works
The Fe/S Assembly Protein IscU Behaves as a Substrate for the Molecular Chaperone Hsc66 from Escherichia coli
Silberg, J. J., Hoff, K. G., Tapley, T. L., & Vickery, L. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009542200 · Cited by 108 · see citing works
Mechanistic studies of the SufS–SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE
de Choudens, S. O., Lascoux, D., Loiseau, L., Barras, F., Forest, É., & Fontecave, M. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01244-4 · Cited by 108 · see citing works
IscA Mediates Iron Delivery for Assembly of Iron-Sulfur Clusters in IscU under the Limited Accessible Free Iron Conditions
Ding, H., Clark, R. J., & Ding, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404533200 · Cited by 108 · see citing works
Network of Protein-Protein Interactions among Iron-Sulfur Cluster Assembly Proteins in Escherichia coli1
Tokumoto, U., Nomura, S., Minami, Y., Mihara, H., Kato, S.-I., Kurihara, T., Esaki, N., Kanazawa, H., Matsubara, H., & Takahashi, Y. (2002) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a003156 · Cited by 107 · see citing works
The Structures of Rieske and Rieske-Type Proteins
Link, T. A. (1999) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60077-x · Cited by 106 · see citing works
Characterization of the NifU and NifS Fe−S Cluster Formation Proteins Essential for Viability in Helicobacter pylori
Olson, J. W., Agar, J. N., Johnson, M. K., & Maier, R. J. (2000) · Biochemistry · doi:10.1021/bi001744s · Cited by 104 · see citing works
Repair of Nitric Oxide-modified Ferredoxin [2Fe-2S] Cluster by Cysteine Desulfurase (IscS)
Yang, W., Rogers, P. A., & Ding, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109485200 · Cited by 104 · see citing works
Cloning and chromosomal mapping of a novel ABC transporter gene (hABC7), a candidate for X-linked sideroblastic anemia with spinocerebellar ataxia
Shimada, Y., Okuno, S., Kawai, A., Shinomiya, H., Saito, A., Suzuki, M., Omori, Y., Nishino, N., Kanemoto, N., Fujiwara, T., et al. (1998) · Journal of Human Genetics · doi:10.1007/s100380050051 · Cited by 102 · see citing works
Iron−Sulfur Cluster Biosynthesis. Kinetic Analysis of [2Fe-2S] Cluster Transfer from Holo ISU to Apo Fd: Role of Redox Chemistry and a Conserved Aspartate
Wu, S., Wu, G. J., Surerus, K. K., & Cowan, J. A. (2002) · Biochemistry · doi:10.1021/bi0256781 · Cited by 101 · see citing works
Sequence-specific Interaction between Mitochondrial Fe-S Scaffold Protein Isu and Hsp70 Ssq1 Is Essential for Their in Vivo Function
Dutkiewicz, R., Schilke, B. A., Cheng, S., Knieszner, H., Craig, E. A., & Marszałek, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402947200 · Cited by 100 · see citing works
SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly
de Choudens, S. O., Sanakis, Y., & Fontecave, M. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0581-9 · Cited by 100 · see citing works
SufA from Erwinia chrysanthemi
de Choudens, S. O., Nachin, L., Sanakis, Y., Loiseau, L., Barras, F., & Fontecave, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300285200 · Cited by 100 · see citing works
Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
Vickery, L. E., Silberg, J. J., & Ta, D. T. (1997) · Protein Science · doi:10.1002/pro.5560060511 · Cited by 99 · see citing works
Two nifA-like genes required for expression of alternative nitrogenases by Azotobacter vinelandii
Joerger, R. D., Jacobson, M. R., & Bishop, P. E. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.6.3258-3267.1989 · Cited by 98 · see citing works
A gene encoding a DnaK/hsp70 homolog in Escherichia coli.
Seaton, B. L., & Vickery, L. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.2066 · Cited by 98 · see citing works
Crystal Structure of the Molecular Chaperone HscA Substrate Binding Domain Complexed with the IscU Recognition Peptide ELPPVKIHC
Cupp‐Vickery, J. R., Peterson, J. C., Ta, D. T., & Vickery, L. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.025 · Cited by 97 · see citing works
Analysis of the E. coli NifS CsdB protein at 2.0 Å reveals the structural basis for perselenide and persulfide intermediate formation
Lima, C. D. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5308 · Cited by 96 · see citing works
Role of the [2Fe−2S] Cluster in Recombinant Escherichia coli Biotin Synthase
Jameson, G. N. L., Cosper, M. M., Hernández, H. L., Johnson, M. K., & Huynh, B. H. (2004) · Biochemistry · doi:10.1021/bi035666v · Cited by 95 · see citing works
Mitochondrial-type iron–sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
LaGier, M. J., Tachezy, J., Stejskal, F., Kutišová, K., & Keithly, J. S. (2003) · Microbiology · doi:10.1099/mic.0.26365-0 · Cited by 94 · see citing works
Crystal Structure of IscA, an Iron-sulfur Cluster Assembly Protein from Escherichia coli
Cupp‐Vickery, J. R., Silberg, J. J., Ta, D. T., & Vickery, L. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.027 · Cited by 92 · see citing works
High-Resolution Structure of the Soluble, Respiratory-Type Rieske Protein fromThermus thermophilus: Analysis and Comparison
Hunsicker‐Wang, L. M., Heine, A., Chen, Y., Luna, E., Todaro, T. R., Zhang, Y., Williams, P. A., McRee, D. E., Hirst, J., Stout, C. D., et al. (2003) · Biochemistry · doi:10.1021/bi0342719 · Cited by 92 · see citing works
Structure of a NifS Homologue: X-ray Structure Analysis of CsdB, an Escherichia coli Counterpart of Mammalian Selenocysteine Lyase,
Fujii, T., Maeda, M., Mihara, H., Kurihara, T., Esaki, N., & Hata, Y. (2000) · Biochemistry · doi:10.1021/bi991732a · Cited by 91 · see citing works
Contributions of the LPPVK Motif of the Iron-Sulfur Template Protein IscU to Interactions with the Hsc66-Hsc20 Chaperone System
Hoff, K. G., Cupp‐Vickery, J. R., & Vickery, L. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305292200 · Cited by 91 · see citing works
The generation of 5′-deoxyadenosyl radicals by adenosylmethionine-dependent radical enzymes
Jarrett, J. T. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(03)00022-x · Cited by 91 · see citing works
Spectroscopic Evidence for a Reduced Fe2S2 Cluster with a S = 9/2 Ground State in Mutant Forms of Clostridium pasteurianum 2Fe Ferredoxin
Crouse, B. R., Meyer, J., & Johnson, M. K. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00142a049 · Cited by 88 · see citing works
A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins
Wollenberg, M., Berndt, C., Bill, E., Schwenn, J. D., & Seidler, A. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03522.x · Cited by 87 · see citing works
The NIFS Protein Can Function as a Selenide Delivery Protein in the Biosynthesis of Selenophosphate
Lacourciere, G. M., & Stadtman, T. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.30921 · Cited by 87 · see citing works
Escherichia coli NifS-like Proteins Provide Selenium in the Pathway for the Biosynthesis of Selenophosphate
Lacourciere, G. M., Mihara, H., Kurihara, T., Esaki, N., & Stadtman, T. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000926200 · Cited by 86 · see citing works
The Hsc66-Hsc20 Chaperone System in Escherichia coli : Chaperone Activity and Interactions with the DnaK-DnaJ-GrpE System
Silberg, J. J., Hoff, K. G., & Vickery, L. E. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.24.6617-6624.1998 · Cited by 86 · see citing works
Characterization of an Iron−Sulfur Cluster Assembly Protein (ISU1) from Schizosaccharomyces pombe
Wu, G. J., Mansy, S. S., Wu, S., Surerus, K. K., Foster, M. W., & Cowan, J. A. (2002) · Biochemistry · doi:10.1021/bi016073s · Cited by 85 · see citing works
Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase
Ugalde, R. A., Imperial, J., Shah, V. K., & Brill, W. J. (1984) · Journal of Bacteriology · doi:10.1128/jb.159.3.888-893.1984 · Cited by 84 · see citing works
Role of the Mitochondrial Hsp70s, Ssc1 and Ssq1, in the Maturation of Yfh1
Voisine, C., Schilke, B. A., Ohlson, M. B., Beinert, H., Marszałek, J., & Craig, E. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3677-3684.2000 · Cited by 84 · see citing works
Mössbauer Study of Cys56Ser Mutant 2Fe Ferredoxin from Clostridium Pasteurianum: Evidence for Double Exchange in an [Fe2S2]+ Cluster
Achim, C., Golinelli‐Cohen, M., Bominaar, E. L., Meyer, J., & Münck, E. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9617698 · Cited by 83 · see citing works
Crystal Structure of the Ancient, Fe−S Scaffold IscA Reveals a Novel Protein Fold
Bilder, P. W., Ding, H., & Newcomer, M. E. (2003) · Biochemistry · doi:10.1021/bi035440s · Cited by 83 · see citing works
The Cysteine Desulfurase IscS Is Required for Synthesis of All Five Thiolated Nucleosides Present in tRNA from Salmonella enterica Serovar Typhimurium
Nilsson, K. L., Lundgren, H. K., Hagervall, T. G., & Björk, G. R. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.24.6830-6835.2002 · Cited by 82 · see citing works
Evidence for Coupled Electron and Proton Transfer in the [8Fe-7S] Cluster of Nitrogenase
Lanzilotta, W. N., Christiansen, J., Dean, D. R., & Seefeldt, L. C. (1998) · Biochemistry · doi:10.1021/bi980048d · Cited by 82 · see citing works
Characterization of the Fundamental Protein Ligand Requirements of [4Fe-4S]2+/+Clusters with Sixteen Amino Acid Maquettes
Mulholland, S. E., Gibney, B. R., Rabanal, F., & Dutton, P. L. (1998) · Journal of the American Chemical Society · doi:10.1021/ja981279a · Cited by 81 · see citing works
Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron–sulfur proteins
Pelzer, W., Mühlenhoff, U., Diekert, K., Siegmund, K., Kispál, G., & Lill, R. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01711-7 · Cited by 81 · see citing works
Iron-Sulfur Cluster Biosynthesis
Mansy, S. S., Wu, G. J., Surerus, K. K., & Cowan, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201439200 · Cited by 81 · see citing works
A Mutant Human IscU Protein Contains a Stable [2Fe−2S]2+ Center of Possible Functional Significance
Foster, M. W., Mansy, S. S., Hwang, J., Penner‐Hahn, J. E., Surerus, K. K., & Cowan, J. A. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000800+ · Cited by 80 · see citing works
Iron−Sulfur Cluster Biosynthesis: Characterization of Iron Nucleation Sites for Assembly of the [2Fe−2S]2+ Cluster Core in IscU Proteins
Nuth, M., Yoon, T., & Cowan, J. A. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0264596 · Cited by 79 · see citing works
J-domain Protein, Jac1p, of Yeast Mitochondria Required for Iron Homeostasis and Activity of Fe-S Cluster Proteins
Kim, R. Y., Saxena, S., Gordon, D. M., Pain, D., & Dancis, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010695200 · Cited by 77 · see citing works
Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1
Wu, G. J., Mansy, S. S., Hemann, C. F., Hille, R., Surerus, K. K., & Cowan, J. A. (2002) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-001-0330-2 · Cited by 75 · see citing works
Nucleotide sequence and genetic analysis of the Azotobacter chroococcum nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine acetyltransferase
Evans, D. J., Jones, R., Woodley, P., Wilborn, J. R., & Robson, R. L. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.17.5457-5469.1991 · Cited by 73 · see citing works
Structure of External Aldimine of Escherichia coli CsdB, an IscS/Nifs Homolog: Implications for Its Specificity toward Selenocysteine
Mihara, H., Fujii, T., Kato, S.-I., Kurihara, T., Hata, Y., & Esaki, N. (2002) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a003151 · Cited by 73 · see citing works
SufC hydrolyzes ATP and interacts with SufB from Thermotoga maritima
Rangachari, K., Davis, C. T., Eccleston, J. F., Hirst, E. M. A., Saldanha, J. W., Strath, M., & Wilson, R. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02369-4 · Cited by 70 · see citing works
The iron-sulfur cluster assembly genes iscS and iscU of Entamoeba histolytica were acquired by horizontal gene transfer
van der Giezen, M., Cox, S. S. E., & Tovar, J. (2004) · BMC Evolutionary Biology · doi:10.1186/1471-2148-4-7 · Cited by 69 · see citing works
The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H
Mihara, H., Kato, S.-I., Lacourciere, G. M., Stadtman, T. C., Kennedy, R., Kurihara, T., Tokumoto, U., Takahashi, Y., & Esaki, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.102176099 · Cited by 69 · see citing works
Metabolic Defects Caused by Mutations in the isc Gene Cluster in Salmonella enterica Serovar Typhimurium: Implications for Thiamine Synthesis
Skovran, E., & Downs, D. M. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.14.3896-3903.2000 · Cited by 69 · see citing works
Crystal structure of the cystine C-S lyase from Synechocystis : Stabilization of cysteine persulfide for FeS cluster biosynthesis
Clausen, T., Kaiser, J. T., Steegborn, C., Huber, R., & Kessler, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.3856 · Cited by 68 · see citing works
Thiamine Biosynthesis in Escherichia coli
Leonardi, R., & Roach, P. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312714200 · Cited by 66 · see citing works
A Modular Domain of NifU, a Nitrogen Fixation Cluster Protein, Is Highly Conserved in Evolution
Hwang, D. M., Dempsey, A. A., Tan, K.-T., & Liew, C. (1996) · Journal of Molecular Evolution · doi:10.1007/bf02337525 · Cited by 65 · see citing works
Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli
Kawula, T. H., & Lelivelt, M. J. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.3.610-619.1994 · Cited by 64 · see citing works
FhuF, an iron‐regulated protein of Escherichia coli with a new type of [2Fe‐2S] center
Müller, K., Matzanke, B. F., Schünemann, V., TRAUTWEIN, A. X., & Hantke, K. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2581001.x · Cited by 63 · see citing works
Thermotoga maritima IscU. Structural Characterization and Dynamics of a New Class of Metallochaperone
Bertini, I., Cowan, J. A., Bianco, C. D., Luchinat, C., & Mansy, S. S. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00768-x · Cited by 63 · see citing works
Staphylococcal NreB: an O 2 ‐sensing histidine protein kinase with an O 2 ‐labile iron–sulphur cluster of the FNR type
Kamps, A., Achebach, S., Fedtke, I., Unden, G., & Götz, F. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04024.x · Cited by 63 · see citing works
Kinetic Characterization of the ATPase Cycle of the Molecular Chaperone Hsc66 from Escherichia coli
Silberg, J. J., & Vickery, L. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7779 · Cited by 61 · see citing works
Crystal Structure of Hsc20, a J-type Co-chaperone from Escherichia coli
Cupp‐Vickery, J. R., & Vickery, L. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4252 · Cited by 60 · see citing works
Purification and Biophysical Characterization of a New [2Fe-2S] Ferredoxin from Azotobacter vinelandii, a Putative [Fe-S] Cluster Assembly/Repair Protein
Jung, Y.-S., Gao-Sheridan, H. S., Christiansen, J., Dean, D. R., & Burgess, B. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32402 · Cited by 59 · see citing works
Comparative organization of nitrogen fixation-specific genes from Azotobacter vinelandii and Klebsiella pneumoniae: DNA sequence of the nifUSV genes
Beynon, J., Ally, A. H., Cannon, M. C., Cannon, F. C., Jacobson, M. R., Cash, V. L., & Dean, D. R. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.9.4024-4029.1987 · Cited by 57 · see citing works
The Cell's Cookbook For Iron–Sulfur Clusters: Recipes For Fool's Gold?
Balk, J., & Lill, R. (2004) · ChemBioChem · doi:10.1002/cbic.200400061 · Cited by 57 · see citing works
Isolation and characterization of polyferredoxin from Methanobacterium thermoautotrophicum The mvhb gene product of the methylviologen‐reducing hydrogenase operon
Hedderich, R., Albracht, S. P. J., Linder, D., Koch, J., & Thauer, R. K. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80023-a · Cited by 56 · see citing works
Azotobacter vinelandii nifD- and nifE -encoded polypeptides share structural homology
Dean, D. R., & Brigle, K. E. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.17.5720 · Cited by 56 · see citing works
Formation of Thiolated Nucleosides Present in tRNA from Salmonella enterica serovar Typhimurium Occurs in Two Principally Distinct Pathways
Leipuvienė, R., Qian, Q., & Björk, G. R. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.3.758-766.2004 · Cited by 55 · see citing works
Ferredoxin:thioredoxin Reductase: Disulfide Reduction Catalyzed via Novel Site-specific [4Fe–4S] Cluster Chemistry
Walters, E. M., & Johnson, M. K. (2004) · Photosynthesis Research · doi:10.1023/b:pres.0000017195.05870.61 · Cited by 55 · see citing works
Mechanism of Cysteine Desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic Analysis of Cleavage of the Persulfide Intermediate by Chemical Reductants
Behshad, E., Parkin, S. E., & Bollinger, J. M., Jr. (2004) · Biochemistry · doi:10.1021/bi049143e · Cited by 55 · see citing works
Biogenesis of iron–sulfur proteins in eukaryotes: components, mechanism and pathology
Gerber, J., & Lill, R. (2002) · Mitochondrion · doi:10.1016/s1567-7249(02)00041-7 · Cited by 54 · see citing works
[35] Escherichia coli SoxR protein: Sensor/transducer of oxidative stress and nitric oxide
Demple, B., Ding, H., & Jorgensen, M. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)48654-5 · Cited by 53 · see citing works
A Novel l-Cysteine/Cystine C-S-Lyase Directing [2Fe-2S] Cluster Formation of SynechocystisFerredoxin
Leibrecht, I., & Kessler, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10442 · Cited by 53 · see citing works
Preferential Substrate Binding Orientation by the Molecular Chaperone HscA
Tapley, T. L., & Vickery, L. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400803200 · Cited by 52 · see citing works
NADH Oxidation by the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae
Türk, K., Puhar, A., Neese, F., Bill, E., Fritz, G., & Steuber, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311692200 · Cited by 52 · see citing works
Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex
Leonardi, R., Fairhurst, S. A., Kriek, M., Lowe, D. J., & Roach, P. L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00204-7 · Cited by 50 · see citing works
Heterodisulfide reductase from Methanothermobacter marburgensis contains an active‐site [4Fe–4S] cluster that is directly involved in mediating heterodisulfide reduction
Duin, E. C., Madadi‐Kahkesh, S., Hedderich, R., Clay, M. D., & Johnson, M. K. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02281-0 · Cited by 50 · see citing works
Substitutions in an Active Site Loop of Escherichia coli IscS Result in Specific Defects in Fe-S Cluster and Thionucleoside Biosynthesis in Vivo
Lauhon, C. T., Skovran, E., Urbina, H. D., Downs, D. M., & Vickery, L. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401261200 · Cited by 50 · see citing works
Identification of a novel prokaryotic HEAT‐repeats‐containing protein which interacts with a cyanobacterial IscA homolog
Morimoto, K., Nishio, K., & Nakai, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02736-9 · Cited by 47 · see citing works
Bacterial IscU is a well folded and functional single domain protein
Adinolfi, S., Rizzo, F. M., Masino, L., Nair, M. M., Martin, S. R., Pastore, A., & Temussi, P. A. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04112.x · Cited by 46 · see citing works
Evidence for Cysteine Persulfide as Reaction Product of l-Cyst(e)ine C-S-Lyase (C-DES) fromSynechocystis
Lang, T., & Kessler, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.189 · Cited by 44 · see citing works
The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1 1 1Edited by M. Yaniv
Schmidt, S., Strub, A., Röttgers, K., Zufall, N., & Voos, W. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5013 · Cited by 40 · see citing works
Extensive Ligand Rearrangements around the [2Fe-2S] Cluster of Clostridium pasteurianum Ferredoxin
Golinelli‐Cohen, M., Chatelet, C., Duin, E. C., Johnson, M. K., & Meyer, J. (1998) · Biochemistry · doi:10.1021/bi9806394 · Cited by 39 · see citing works
Role of Cluster-Ligated Aspartate in Gating Electron Transfer in the Four-Iron Ferredoxin from the Hyperthermophilic Archaeon Pyrococcus furiosus
Calzolai, L., Zhou, Z. H., Adams, M. W. W., & Mar, G. N. L. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953744z · Cited by 38 · see citing works
A paradigm for biological sulfur transfers via persulfide groups: a persulfide–disulfide–thiol cycle in 4-thiouridine biosynthesis
Wright, C. M., Palenchar, P. M., & Mueller, E. G. (2002) · Chemical Communications · doi:10.1039/b208626c · Cited by 38 · see citing works

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Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,571 · see citing works
Structure/Function Relationships of [NiFe]- and [FeFe]-Hydrogenases
Fontecilla-Camps, J. C., Volbeda, A., Cavazza, C., & Nicolet, Y. (2007) · Chemical Reviews · doi:10.1021/cr050195z · Cited by 1,339 · see citing works
Function and biogenesis of iron-sulphur proteins
Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167 · see citing works
The role of iron regulatory proteins in mammalian iron homeostasis and disease
Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055 · see citing works
“Mammalian iron-sulfur cluster assembly Assembly of iron-sulfur clusters is a complex process involving many enzymes and scaffold protein”
Background
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872 · see citing works
“NifS is a pyridoxal phosphate-dependent cysteine desulphurase and is responsible for the formation of a protein-bound cysteine persulphide that is subsequently donated to NifU for the sequential formation of [2Fe–2S] and [4Fe–4S] cluster”
Background
Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
Liu, J., Chakraborty, S., Hosseinzadeh, P., Yu, Y., Tian, S., Petrik, I. D., Bhagi, A., & Lu, Y. (2014) · Chemical Reviews · doi:10.1021/cr400479b · Cited by 881 · see citing works
Evolution of Photosynthesis
Hohmann-Marriott, M. F., & Blankenship, R. E. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042110-103811 · Cited by 744 · see citing works
“FeS clusters (90) mediate electron transport in photosynthesis and respiration, including ferredoxins (4Fe-4S, 3Fe-4S, 2Fe-2S) and Rieske FeS clusters.”
Background
Iron‐sulphur clusters and the problem with oxygen
Imlay, J. A. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05028.x · Cited by 717 · see citing works
The N‐end rule pathway and regulation by proteolysis
Varshavsky, A. J. (2011) · Protein Science · doi:10.1002/pro.666 · Cited by 696 · see citing works
Lag Phase Is a Distinct Growth Phase That Prepares Bacteria for Exponential Growth and Involves Transient Metal Accumulation
Rolfe, M. D., Rice, C. J., Lucchini, S., Pin, C., Thompson, A., Cameron, A. D. S., Alston, M., Stringer, M. F., Betts, R. P., Baranyi, J., et al. (2012) · Journal of Bacteriology · doi:10.1128/jb.06112-11 · Cited by 711 · see citing works
“Many metabolic and respiratory proteins, such as aconitases (AcnA, AcnB) and succinate dehydrogenase (SdhB), contain Fe-S clusters that are essential for enzyme activity (16, 54, 112).”
Background
Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases
Lill, R., & Mühlenhoff, U. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162653 · Cited by 595 · see citing works
Mammalian iron metabolism and its control by iron regulatory proteins
Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works
The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 501 · see citing works
Biosynthesis of the Iron-Molybdenum Cofactor of Nitrogenase
Rubio, L. M., & Ludden, P. W. (2008) · Annual Review of Microbiology · doi:10.1146/annurev.micro.62.081307.162737 · Cited by 492 · see citing works
Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli
Dwyer, D. J., Kohanski, M. A., Hayete, B., & Collins, J. J. (2007) · Molecular Systems Biology · doi:10.1038/msb4100135 · Cited by 470 · see citing works
“S catalysis, evolutionarily related to the oxygen-free and iron-and sulfur-rich environment that existed billions of years ago (Johnson et al , 2005; Imlay, 2006), has predisposed these organisms to oxidative damage.”
Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis
Lill, R., & Freibert, S.-A. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111540 · Cited by 453 · see citing works
Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression
Chen, Z., Li, Y., Zhang, H., Huang, P., & Luthra, R. (2010) · Oncogene · doi:10.1038/onc.2010.193 · Cited by 426 · see citing works
“ISCU is essential for the assembly of Fe-S clusters, which are major components in the mitochondrial electron transport chain/tricarboxylic acid cycle and define the electron transport pathways in redox enzymes (Johnson et al., 2005).”
Background
Photobiocatalysis: Activating Redox Enzymes by Direct or Indirect Transfer of Photoinduced Electrons
Lee, S. H., Choi, D. S., Kuk, S. K., & Park, C. B. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201710070 · Cited by 423 · see citing works
Chemistry of Iron N -Heterocyclic Carbene Complexes: Syntheses, Structures, Reactivities, and Catalytic Applications
Riener, K., Haslinger, S., Raba, A., Högerl, M. P., Cokoja, M., Herrmann, W. A., & Kühn, F. E. (2014) · Chemical Reviews · doi:10.1021/cr4006439 · Cited by 411 · see citing works
Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis
Sheftel, A. D., Stehling, O., Pierik, A. J., Elsässer, H.-P., Mühlenhoff, U., Webert, H., Hobler, A., Hannemann, F., Bernhardt, R., & Lill, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004250107 · Cited by 406 · see citing works
“of a truncated bovine adrenodoxin, Adx(4-108).”
Influential
Iron–sulfur cluster biogenesis and trafficking in mitochondria
Braymer, J. J., & Lill, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.787101 · Cited by 389 · see citing works
“These cofactors participate in electron transfer reactions, Lewis acid catalysis, transfer of sulfur atoms, or facilitating structural roles (5, 6).”
Background
Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease
Lane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399 · see citing works
Iron–sulfur cluster biogenesis and human disease
Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 387 · see citing works
“[ 1 ,2]). The most common Fe–S clusters in eukaryotes are the [2Fe–2S] and [4Fe–4S] clusters, which are formed by tetrahedrally coordinated iron atoms with bridging sulfides and are most often ligated to the protein through cysteine residues.”
BackgroundInfluential
Heme Synthesis and Acquisition in Bacterial Pathogens
Choby, J. E., & Skaar, E. P. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.018 · Cited by 343 · see citing works
Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms
Lill, R., & Mühlenhoff, U. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104538 · Cited by 365 · see citing works
“For a more comprehensive summary of the complex and diverse pathways of bacterial Fe/S protein assembly, we direct the reader to recent excellent reviews (Mansy & Cowan 2004, Barras et al. 2005, Fontecave et al. 2005, Johnson et al. 2005).”
BackgroundMethodInfluential
Maturation of Hydrogenases
Böck, A., King, P. W., Blokesch, M., & Posewitz, M. C. (2006) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(06)51001-x · Cited by 353 · see citing works
Methylerythritol Phosphate Pathway of Isoprenoid Biosynthesis
Zhao, L., Chang, W., Xiao, Y., Liu, H., & Liu, P. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052010-100934 · Cited by 356 · see citing works
Trafficking in persulfides: delivering sulfur in biosynthetic pathways
Mueller, E. G. (2006) · Nature Chemical Biology · doi:10.1038/nchembio779 · Cited by 351 · see citing works
“For the synthesis of iron-sulfur clusters, the persulfide group is transferred to a scaffold protein (IscU, for example), where a nascent iron-sulfur cluster is assembled for transfer to an apo-enzyme that requires an iron-sulfur cluster for activit”
Background
Fe-S Cluster Assembly Pathways in Bacteria
Ayala-Castro, C. N., Saini, A. K., & Outten, F. W. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00034-07 · Cited by 343 · see citing works
“scaffolds, which are not usually encoded with HscA or HscB, suggesting that SufU and NifU either do not require molecular chaperones or utilize a completely separate chaperone system (46).”
BackgroundInfluential
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.2012.12.010 · Cited by 335 · see citing works
Low-energy spectrum of iron–sulfur clusters directly from many-particle quantum mechanics
Sharma, S., Sivalingam, K., Neese, F., & Chan, G. K. (2014) · Nature Chemistry · doi:10.1038/nchem.2041 · Cited by 314 · see citing works
Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydAΔEFG
Mulder, D. W., Boyd, E. S., Sarma, R., Spietz, R. L., Endrizzi, J. A., Broderick, J. B., & Peters, J. W. (2010) · Nature · doi:10.1038/nature08993 · Cited by 307 · see citing works
The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works
“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 a…”
Background
An overview of molecular basis of iron metabolism regulation and the associated pathologies
Silva, B., & Faustino, P. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.03.011 · Cited by 300 · see citing works
“During iron de ﬁ ciency, IRP1 binds to IRE through a cavity on its structure, while under iron overload that same cavity is occupied by the 4Fe – 4S cluster and unavailable to bind to the IRE [137,138].”
Background
Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
Tong, W.-H., & Rouault, T. A. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.003 · Cited by 294 · see citing works
“Much of what is known about Fe-S cluster biogenesis comes from the extensive genetic and biochemical studies of gene products of the bacterial nif, isc, and suf operons and their homologs in S. cerevisiae (Johnson et al., 2005; Lill and Muhlenhoff, 2005).”
Background
A Fatal Mitochondrial Disease Is Associated with Defective NFU1 Function in the Maturation of a Subset of Mitochondrial Fe-S Proteins
Navarro‐Sastre, A., Tort, F., Stehling, O., Uzarska, M. A., Arranz, J. A., del Toro, M., Labayru, M. T., Landa, J., Font, A., García‐Villoria, J., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.10.005 · Cited by 283 · see citing works
Human Frataxin Is an Allosteric Switch That Activates the Fe−S Cluster Biosynthetic Complex
Tsai, C.-L., & Barondeau, D. P. (2010) · Biochemistry · doi:10.1021/bi1013062 · Cited by 282 · see citing works
“In vitro, iron and sulfide can be used to chemically synthesize Fe-S clusters or activate Fe-S apoproteins (1, 2).”
Background
Cytosolic Monothiol Glutaredoxins Function in Intracellular Iron Sensing and Trafficking via Their Bound Iron-Sulfur Cluster
Mühlenhoff, U., Molik, S., Godoy, J. R., Uzarska, M. A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.001 · Cited by 276 · see citing works
“This striking result for C171S Grx4-Myc may be explained on the basis of earlier observations showing that, in some cases, Ser (but not Ala) may function as a (weak) ligand for iron (da Silva and Williams, 2001; Johnson et al., 2005).”
IscR‐dependent gene expression links iron‐sulphur cluster assembly to the control of O 2 ‐regulated genes in Escherichia coli
Giel, J. L., Rodionov, D. A., Liu, M., Blattner, F. R., & Kiley, P. J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05160.x · Cited by 276 · see citing works
Metabolic maps and functions of thePlasmodiummitochondrion
van Dooren, G. G., Stimmler, L. M., & McFadden, G. I. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00027.x · Cited by 272 · see citing works
“150), ISU (PF14_0518) and two homologues of ISA (PFB0320c and PFC1005c) (Fig.”
Influential
Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions
Shi, R., Proteau, A., Villarroya, M., Moukadiri, I., Zhang, L., Trempe, J., Matte, A., Armengod, M. ‐., & Cygler, M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000354 · Cited by 270 · see citing works
“The enzymes TtcA and MiaB accept sulfur from IscU [3] and are responsible for the s(2)C32 [25] and ms(2)i(o)(6)A37 modification [26], respectively.”
Background
An Endoperoxide Reactivity-Based FRET Probe for Ratiometric Fluorescence Imaging of Labile Iron Pools in Living Cells
Aron, A. T., Loehr, M. O., Bogena, J., & Chang, C. J. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b08016 · Cited by 269 · see citing works
Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters
Bandyopadhyay, S., Gama, F., Molina‐Navarro, M. M., Gualberto, J. M., Claxton, R., Naik, S., Huynh, B. H., Herrero, E., Jacquot, J., Johnson, M. K., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.50 · Cited by 267 · see citing works
“…from investigation of components of the bacterial isc (iron–sulphur cluster assembly), suf (sulfur mobilization) and nif (nitrogen fixation) operons (Johnson et al, 2005) and identification and characterization of homologous ISC-type proteins in yeast and mammalian mitochondria (Lill and…”
Background
Iron–sulfur protein folds, iron–sulfur chemistry, and evolution
Meyer, J. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0318-7 · Cited by 266 · see citing works
Transition metals in plant photosynthesis
Yruela, I. (2013) · Metallomics · doi:10.1039/c3mt00086a · Cited by 262 · see citing works
Iron-Sulfur Cluster Biosynthesis
Layer, G., de Choudens, S. O., Sanakis, Y., & Fontecave, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513569200 · Cited by 257 · see citing works
Emerging critical roles of Fe–S clusters in DNA replication and repair
Fuss, J. O., Tsai, C.-L., Ishida, J. P., & Tainer, J. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.018 · Cited by 253 · see citing works
“Fe-S clusters are best known for their activities in oxidation-reduction reactions of mitochondrial electron transport, catalysis by aconitase, generation of radicals by SAMdependent enzymes, and sulfur donors in biosynthesis [22].”
Background
Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
Adinolfi, S., Iannuzzi, C., Prischi, F., Pastore, C., Iametti, S., Martin, S. R., Bonomi, F., & Pastore, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1579 · Cited by 256 · see citing works
“In this assay, the cluster is formed under strict anaerobic conditions on the scaffold protein IscU, either chemically, using sulfide and ferric ammonium citrate as sources of sulfur and iron, respectively, or enzymaticall”
Method
Staphylococcal response to oxidative stress
Gaupp, R., Ledala, N., & Somerville, G. A. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00033 · Cited by 253 · see citing works
Biogenesis of iron–sulfur proteins in plants
Balk, J., & Lobréaux, S. (2005) · Trends in Plant Science · doi:10.1016/j.tplants.2005.05.002 · Cited by 246 · see citing works
Developments in the Biomimetic Chemistry of Cubane-Type and Higher Nuclearity Iron–Sulfur Clusters
Lee, S. C., Lo, W., & Holm, R. H. (2014) · Chemical Reviews · doi:10.1021/cr4004067 · Cited by 246 · see citing works
Oxidative Stress in Bacteria and the Central Dogma of Molecular Biology
Fasnacht, M., & Polacek, N. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.671037 · Cited by 246 · see citing works
“Their functions are extremely versatile, ranging from simple iron storage to the regulation of gene expression (Johnson et al., 2005).”
Background
Copper Stress Affects Iron Homeostasis by Destabilizing Iron-Sulfur Cluster Formation in Bacillus subtilis
Chillappagari, S., Seubert, A., Trip, H., Kuipers, O. P., Marahiel, M. A., & Miethke, M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00058-10 · Cited by 239 · see citing works
“coli, possessing both the constitutive ISC and the stress-dependent SUF cluster biogenesis systems (26), is generally less susceptible to copper stress than B.”
Background
The pathogenesis of Friedreich ataxia and the structure and function of frataxin
Pandolfo, M., & Pastore, A. (2009) · Journal of Neurology · doi:10.1007/s00415-009-1003-2 · Cited by 242 · see citing works
“IscU (or Isu in eukaryotes) is the scaffold on which the cluster is transiently assembled [ 69 ].”
Background
Iron-sulfur clusters: ever-expanding roles
Fontecave, M. (2006) · Nature Chemical Biology · doi:10.1038/nchembio0406-171 · Cited by 225 · see citing works
[FeFe] hydrogenases and their evolution: a genomic perspective
Meyer, J. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6477-4 · Cited by 242 · see citing works
“Regarding the accessory Fe-S clusters, previous work suggests that their assembly is independent of the biosynthesis of the active site [9, 44], and most probably carried out by the Isc or Suf systems [ 45 ].”
BackgroundMethod
Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts
Ye, H., Jeong, S. Y., Ghosh, M. C., Kovtunovych, G., Silvestri, L., Ortillo, D., Uchida, N., Tisdale, J. F., Camaschella, C., & Rouault, T. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40372 · Cited by 239 · see citing works
Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes
Kessler, D. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00036.x · Cited by 239 · see citing works
“IscA is suggested to be either an alternative scaffold protein or to have some role in iron delivery to IscU (Ding et al., 2005), HscB and HscA are specialized chaperones, and Fdx is a 2Fe–2S ferredoxin with an as yet poorly defined redox role (Johnson et al., 2005).”
BackgroundMethodInfluential
Human Iron−Sulfur Cluster Assembly, Cellular Iron Homeostasis, and Disease
Ye, H., & Rouault, T. A. (2010) · Biochemistry · doi:10.1021/bi1004798 · Cited by 238 · see citing works
“identified initially in nitrogen-fixing bacteria, and subsequently in Escherichia coli and other bacteria (17).”
Background
Mechanistic concepts of iron-sulfur protein biogenesis in Biology
Braymer, J. J., Freibert, S., Rakwalska‐Bange, M., & Lill, R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118863 · Cited by 233 · see citing works
Mammalian Frataxin: An Essential Function for Cellular Viability through an Interaction with a Preformed ISCU/NFS1/ISD11 Iron-Sulfur Assembly Complex
Schmucker, S., Martelli, A., Colin, F., Page, A., Wattenhofer‐Donzé, M., Reutenauer, L., & Puccio, H. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016199 · Cited by 234 · see citing works
“Within the past decade, the biogenesis of Fe-S proteins has been extensively studied in bacteria and yeast demonstrating that it is a complex process involving multiple highly conserved components [17,18].”
Background
Localization and functionality of microsporidian iron–sulphur cluster assembly proteins
Goldberg, A. V., Molik, S., Tsaousis, A. D., Neumann, K., Kuhnke, G., Delbac, F., Vivarès, C. P., Hirt, R. P., Lill, R., & Embley, T. M. (2008) · Nature · doi:10.1038/nature06606 · Cited by 230 · see citing works
Regulation of Iron Homeostasis and Use in Chloroplasts
Kroh, G. E., & Pilon, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093395 · Cited by 231 · see citing works
The Role of Mitochondria in Cellular Iron-Sulfur Protein Biogenesis: Mechanisms, Connected Processes, and DiseasesPreprint
Stehling, O., & Lill, R. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011312 · Cited by 228 · see citing works
“The fact that the basic mechanism of mitochondrial ISC assembly has been inherited in evolution from the bacterial ancestor of the organelles has been useful to transfer functional insights from studying the related bacterial ISC assembly system to the eukaryotic situation (Johnson et al. 2005; Bandyopadhyay et al. 20…”
Monothiol glutaredoxins: a common domain for multiple functions
Herrero, E., & de la Torre-Ruiz, M. Á. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6554-8 · Cited by 226 · see citing works
Genetic Screen for Cell Fitness in High or Low Oxygen Highlights Mitochondrial and Lipid Metabolism
Jain, I. H., Calvo, S. E., Markhard, A. L., Skinner, O. S., To, T.-L., Ast, T., & Mootha, V. K. (2020) · Cell · doi:10.1016/j.cell.2020.03.029 · Cited by 224 · see citing works
“For example, it is known that Fe-S clusters can form spontaneously under anaerobic conditions, but in the presence of oxygen, require enzymatic synthesis (Imlay, 2006; Johnson et al., 2005).”
Essential role of Isd11 in mitochondrial iron–sulfur cluster synthesis on Isu scaffold proteins
Wiedemann, N., Urzica, E. I., Guiard, B., Müller, H., Lohaus, C., Meyer, H. E., Ryan, M. T., Meisinger, C., Mühlenhoff, U., Lill, R., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600906 · Cited by 224 · see citing works
“…machinery contain homologs/correlates in the bacterial ISC, NIF and SUF systems for Fe/S cluster biogenesis, while the majority of essential components of the protein import machinery are specific for eukaryotic cells (Pfanner et al, 2004; Johnson et al, 2005; Lill and Mühlenhoff, 2005).”
Background
Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex
Boniecki, M. T., Freibert, S., Mühlenhoff, U., Lill, R., & Cygler, M. (2017) · Nature Communications · doi:10.1038/s41467-017-01497-1 · Cited by 221 · see citing works
IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe‐S assembly proteins
Yeo, W., Lee, J., Lee, K., & Roe, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05220.x · Cited by 218 · see citing works
“The biogenesis of Fe-S clusters have been studied extensively in bacteria, and the mitochondria and plastids of eukaryotes (Frazzon and Dean, 2003; Johnson et al., 2005; Lill and Mühlenhoff, 2005).”
Background
Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery
Maio, N., & Rouault, T. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.009 · Cited by 215 · see citing works
“It binds target proteins that contain the LYR motif [Fe-S] cluster transfer SIL1 (BAP) Mge1 Nucleotide exchange factor [Fe-S] cluster transfer GLRX5 Grx5 Intermediate carrier [Fe-S] cluster transfer- late acting factor ISCA1 Isa1 [Fe4-S4] assembly [Fe-S] cluster transfer- late acting factor ISCA2 Isa2 [Fe4-S4] assembl…”
BackgroundInfluential
Discovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis
Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 213 · see citing works
“…selected ISCA1 (yeast ISA1) and C1orf69 (yeast IBA57), which are known to participate in the maturation of Fe-S clusters essential for the activity of a specific subset of mitochondria proteins (Gelling et al., 2008; Johnson et al., 2005), but have not been directly implicated in heme biosynthesis.”
The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation
Sheftel, A. D., Wilbrecht, C., Stehling, O., Niggemeyer, B., Elsässer, H., Mühlenhoff, U., & Lill, R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0772 · Cited by 213 · see citing works
“Among other components of Fe/S protein assembly, the isc and suf operons of bacteria encode the so-called A-type iron–sulfur cluster (ISC) proteins IscA and SufA, respectively, which are involved in the maturation of bacterial [4Fe-4S] proteins (Johnson et al., 2005; Tan et al., 2009).”
Background
Analytical measurement of discrete hydrogen sulfide pools in biological specimens
Shen, X., Peter, E. A., Bir, S., Wang, R., & Kevil, C. G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.007 · Cited by 214 · see citing works
“Acid-labile sulfide, the other major pool, consists of sulfur present in the iron–sulfur clusters contained in iron–sulfur proteins (nonheme), which are ubiquitous in living organisms and include a variety of proteins and enzymes including rubredoxins, ferredoxins, aconitase, and succinate dehydrogenase [10,12].”
Background
Class I Ribonucleotide Reductases: Metallocofactor Assembly and Repair In Vitro and In Vivo
Cotruvo, J. A., & Stubbe, J. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061408-095817 · Cited by 212 · see citing works
“Pioneering studies of the Dean group (2), followed by work from many labs, have contributed to our understanding of iron-sulfur (FeS) cluster biosynthesis and the complex machinery required (reviewed in Reference 6).”
Background
Variation in vine vigour, grape yield and vineyard soils and topography as indicators of variation in the chemical composition of grapes, wine and wine sensory attributes
Bramley, R. G. V., Ouzman, J., & Boss, P. K. (2011) · Australian Journal of Grape and Wine Research · doi:10.1111/j.1755-0238.2011.00136.x · Cited by 211 · see citing works
Glutaredoxins: roles in iron homeostasis
Rouhier, N., Couturier, J., Johnson, M. K., & Jacquot, J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.08.005 · Cited by 209 · see citing works
Biological chemistry of hydrogen sulfide and persulfides
Cuevasanta, E., Möller, M. N., & Álvarez, B. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.09.018 · Cited by 202 · see citing works
Iron–Sulfur Clusters as Biological Sensors: The Chemistry of Reactions with Molecular Oxygen and Nitric Oxide
Crack, J. C., Green, J. D., THOMSON, A. J., & Brun, N. E. L. (2014) · Accounts of Chemical Research · doi:10.1021/ar5002507 · Cited by 204 · see citing works
Review of recent progress in the study of corrosion products of steels in a hydrogen sulphide environment
Wen, X., Bai, P., Luo, B., Zheng, S., & Chen, C. (2018) · Corrosion Science · doi:10.1016/j.corsci.2018.05.002 · Cited by 203 · see citing works
Iron–sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
Fontecave, M., & de Choudens, S. O. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.12.014 · Cited by 202 · see citing works
Mammalian iron-sulphur proteins: novel insights into biogenesis and function
Rouault, T. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3909 · Cited by 201 · see citing works
Iron–sulfur proteins in health and disease
Sheftel, A. D., Stehling, O., & Lill, R. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.12.006 · Cited by 203 · see citing works
Cobalt Stress in Escherichia coli
Ranquet, C., de Choudens, S. O., Loiseau, L., Barras, F., & Fontecave, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702519200 · Cited by 199 · see citing works
Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme
Zhang, Y., Zhu, X., Torelli, A. T., Lee, M., Dzikovski, B. G., Koralewski, R. M., Wang, E., Freed, J. H., Krebs, C., Ealick, S. E., et al. (2010) · Nature · doi:10.1038/nature09138 · Cited by 198 · see citing works
“The Fe-S cluster assembly pathways in bacteria and mitochondria of eukaryotes are known to involve J domain-containing co-chaperone proteins, such as bacterial HscB and yeast JAC1 37 , 38 , that are similar to DPH4.”
Current Therapeutics, Their Problems, and Sulfur-Containing-Amino-Acid Metabolism as a Novel Target against Infections by “Amitochondriate” Protozoan Parasites
Ali, V., & Nozaki, T. (2007) · Clinical Microbiology Reviews · doi:10.1128/cmr.00019-06 · Cited by 198 · see citing works
“Fe-S clusters have various important functions, including oxidative phosphorylation, electron transfer, and regulation of gene expression and of enzyme activities including substrate binding and activation, sulfur donation, and iron storage (27, 152).”
Background
The diverse roles of J-proteins, the obligate Hsp70 co-chaperone
Craig, E. A., Huang, P., Aron, R., & Andrew, A. J. (2006) · Springer eBooks · doi:10.1007/s10254-005-0001-0 · Cited by 198 · see citing works
“Both eukaryotes and prokaryotes have specialized systems for the assembly of Fe-S centers, an essential prosthetic group for certain proteins ( Johnson et al. 2005; Lill and Muhlenhoff 2005).”
Background
<i>Mycobacterium tuberculosis</i> WhiB3 responds to O <sub>2</sub> and nitric oxide via its [4Fe-4S] cluster and is essential for nutrient starvation survival
Singh, A., Guidry, L., Narasimhulu, K. V., Mai, D., Trombley, J., Redding, K. E., Giles, G. I., Lancaster, J. R., & Steyn, A. J. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700490104 · Cited by 194 · see citing works
The role of iron in mitochondrial function
Levi, S., & Rovida, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.008 · Cited by 195 · see citing works
Iron-Sulfur (Fe/S) Protein Biogenesis: Phylogenomic and Genetic Studies of A-Type Carriers
Vinella, D., Brochier‐Armanet, C., Loiseau, L., Talla, E., & Barras, F. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000497 · Cited by 191 · see citing works
“sufA iscA Conditional Lethality Is Most Likely Due to Insufficient Maturation of IPP Synthesizing Enzymes IspG/H The iscA and sufA single mutants have repeatedly been found to cause marginal defects [5,6].”
Background
Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis
Netz, D. J. A., Stümpfig, M., Doré, C., Mühlenhoff, U., Pierik, A. J., & Lill, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.432 · Cited by 189 · see citing works
“432" language="eng" relation="no"> Iron-sulfur clusters (Fe-S) are inorganic cofactors of proteins involved in a multitude of essential cellular processes such as electron transfer, enzymatic catalysis, gene regulation, ribosome synthesis, tRNA modification, and DNA replication and repai”
Background
The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions
Couturier, J., Touraine, B., Briat, J., Gaymard, F., & Rouhier, N. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00259 · Cited by 189 · see citing works
Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation
Vickery, L. E., & Cupp‐Vickery, J. R. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701322298 · Cited by 188 · see citing works
“…of genetic and biochemical approaches have led to the identification of three types of systems involved in [FeS]-cluster assembly and maturation, and each contains a group of highly specialized proteins (see reviews by Johnson et al., 2005; Mühlenhoff and Lill, 2006; Rouault and Tong, 2005).”
Background
FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster
Wang, H., Shi, H., Rajan, M., Canarie, E. R., Hong, S., Simoneschi, D., Pagano, M., Bush, M. F., Stoll, S., Leibold, E. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.011 · Cited by 185 · see citing works
“Iron-sulfur clusters have long been documented to play critical roles in a variety of biological regulatory mechanisms by sensing the levels of different physiological factors (Johnson et al., 2005; Lill, 2009; Rouault, 2015).”
Background
Structural bases for the interaction of frataxin with the central components of iron–sulphur cluster assembly
Prischi, F., Konarev, P. V., Iannuzzi, C., Pastore, C., Adinolfi, S., Martin, S. R., Svergun, D. I., & Pastore, A. (2010) · Nature Communications · doi:10.1038/ncomms1097 · Cited by 186 · see citing works
“7), which catalyses the reaction that converts l-cysteine into alanine and a highly reactive sulphide, and the scaffold protein on which the cluster is transiently forme”
Background
Fluorescent probes for ferroptosis bioimaging: advances, challenges, and prospects
Yin, J., Zhan, J., Hu, Q., Huang, S., & Lin, W. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00454b · Cited by 181 · see citing works
A review of the effects of iron compounds on methanogenesis in anaerobic environments
Baek, G., Kim, J., & Lee, C. (2019) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2019.109282 · Cited by 185 · see citing works
SufE Transfers Sulfur from SufS to SufB for Iron-Sulfur Cluster Assembly
Layer, G., Gaddam, S. A., Ayala-Castro, C. N., de Choudens, S. O., Lascoux, D., Fontecave, M., & Outten, F. W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608555200 · Cited by 182 · see citing works
Genetic Architecture of Intrinsic Antibiotic Susceptibility
Girgis, H. S., Hottes, A. K., & Tavazoie, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005629 · Cited by 178 · see citing works
“The media used lacks cysteine, the sulfur donor for iron-sulfur center synthesis [88], so disruption of cysteine biosynthesis should reduce the availability of sulfur for iron-sulfur centers.”
Background
Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin
Webert, H., Freibert, S., Gallo, A., Heidenreich, T., Linne, U., Amlacher, S., Hurt, E., Mühlenhoff, U., Banci, L., & Lill, R. (2014) · Nature Communications · doi:10.1038/ncomms6013 · Cited by 177 · see citing works

Iron–sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
Fontecave, M., & de Choudens, S. O. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.12.014 · Cited by 202 · see citing works
Research Progress on Structure,Function,and Biosynthesis of Iron-sulfur Cluster
Liu, J. (2008) · Xiandai shengwu yixue jinzhan
Iron–sulfur cluster biosynthesis
Bandyopadhyay, S., Chandramouli, K., & Johnson, M. K. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361112 · Cited by 169 · see citing works
Feedback regulation of iron-sulfur cluster biosynthesis
Jeverson Frazzon, B., & Dean, D. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011579098 · Cited by 29 · see citing works
Intricacies in iron–sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity
Spigelmyer, S. M., & Santos, P. C. D. (2026) · RSC Chemical Biology · doi:10.1039/d5cb00330j · Cited by 2 · see citing works

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: Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Materials Science › Materials Chemistry › 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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