Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms

Global analysis of protein expression in yeast

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Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

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Iron-sulfur clusters: nature's modular, multipurpose structures

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Balancing Acts

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

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The WD repeat: a common architecture for diverse functions

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Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin

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Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits

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The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins

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Assembly of Iron-Sulfur Clusters

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Nitric oxide‐induced bacteriostasis and modification of iron‐sulphur proteins in Escherichia coli

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Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis

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Low aerobic mitochondrial energy metabolism in poorly- or undifferentiated neuroblastoma

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The emerging role of iron dyshomeostasis in the mitochondrial decay of aging

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Recent advances in the understanding of inherited sideroblastic anaemia

Camaschella, C. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07290.x · Cited by 79

A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis

Song, D., & Lee, F. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708077200 · Cited by 79

Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe–S Assembly Complex

Fox, N. G., Das, D., Chakrabarti, M., Lindahl, P. A., & Barondeau, D. P. (2015) · Biochemistry · doi:10.1021/bi5014497 · Cited by 76

From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis

Lill, R. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0117 · Cited by 73

Loss of Cardiolipin Leads to Perturbation of Mitochondrial and Cellular Iron Homeostasis

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The Essentials of Protein Import in the Degenerate Mitochondrion of Entamoeba histolytica

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A Novel Group of Glutaredoxins in thecis-Golgi Critical for Oxidative Stress Resistance

Mesecke, N., Spang, A., Deponte, M., & Herrmann, J. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0896 · Cited by 72

Effect of mitochondrial complex I inhibition on Fe–S cluster protein activity

Mena, N. P., Bulteau, A., Salazar, J., Hirsch, É. C., & Núñez, M. T. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.137 · Cited by 71

Monothiol glutaredoxin Grx5 interacts with Fe–S scaffold proteins Isa1 and Isa2 and supports Fe–S assembly and DNA integrity in mitochondria of fission yeast

Kim, K.-D., Chung, W., Kim, H.-J., Lee, K.-C., & Roe, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.051 · Cited by 71

Mitochondrial Iron Metabolism: The Crucial Actors in Diseases

Duan, G., Li, J., Duan, Y., Zheng, C., Guo, Q., Li, F., Zheng, J., Yu, J., Zhang, P., Wan, M., et al. (2022) · Molecules · doi:10.3390/molecules28010029 · Cited by 74

Metabolomic Profiling of Human Spermatozoa in Idiopathic Asthenozoospermia Patients Using Gas Chromatography-Mass Spectrometry

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A G-protein editor gates coenzyme B 12 loading and is corrupted in methylmalonic aciduria

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Thio Modification of Yeast Cytosolic tRNA Is an Iron-Sulfur Protein-Dependent Pathway

Nakai, Y., Nakai, M., Lill, R., Suzuki, T., & Hayashi, H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01321-06 · Cited by 66

A novel pyrene based fluorescent probe for selective detection of cysteine in presence of other bio-thiols in living cells

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Mitochondrial Quality Control via Mitochondrial Unfolded Protein Response (mtUPR) in Ageing and Neurodegenerative Diseases

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Elucidation of the interplay between Fe(II), Fe(III), and dopamine with relevance to iron solubilization and reactive oxygen species generation by catecholamines

Sun, Y., Pham, A. N., & Waite, T. D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13615 · Cited by 65

Saccharomyces cerevisiae Grx6 and Grx7 Are Monothiol Glutaredoxins Associated with the Early Secretory Pathway

Izquierdo, A., Casas, C., Mühlenhoff, U., Lillig, C. H., & Herrero, E. (2008) · Eukaryotic Cell · doi:10.1128/ec.00133-08 · Cited by 66

EPR and Mössbauer Spectroscopy of Intact Mitochondria Isolated from Yah1p-DepletedSaccharomyces cerevisiae

Miao, R., Martinho, M., Morales, J. G., Kim, H., Ellis, E. A., Lill, R., Hendrich, M. P., Münck, E., & Lindahl, P. A. (2008) · Biochemistry · doi:10.1021/bi801047q · Cited by 62

Interaction of l -Cysteine with ZnO: Structure, Surface Chemistry, and Optical Properties

Sandmann, A., Kompch, A., Mackert, V., Liebscher, C. H., & Winterer, M. (2015) · Langmuir · doi:10.1021/la504968m · Cited by 61

Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly

Cai, K., Frederick, R. O., Tonelli, M., & Markley, J. L. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.03.007 · Cited by 64

Iron regulation by hepatocytes and free radicals

Takami, T., & Sakaida, I. (2011) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.10-76 · Cited by 60

Iron-sulfur clusters in mitochondrial metabolism: Multifaceted roles of a simple cofactor

Stiban, J., So, M., & Kaguni, L. S. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916100059 · Cited by 61

The cytosolic Fe-S cluster assembly component MET18 is required for the full enzymatic activity of ROS1 in active DNA demethylation

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Factors affecting yeast ethanol tolerance and fermentation efficiency

Vamvakas, S. M., & Kapolos, J. (2020) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-020-02881-8 · Cited by 66

Malfunctioning of the Iron–Sulfur Cluster Assembly Machinery in Saccharomyces cerevisiae Produces Oxidative Stress via an Iron-Dependent Mechanism, Causing Dysfunction in Respiratory Complexes

Gómez-Gallardo, M., Pérez‐Gallardo, R. V., Sánchez, L. A., Díaz-Pérez, A. L., Cortés‐Rojo, C., Carmen, V. M., Saavedra‐Molina, A., Lara‐Romero, J., Jiménez‐Sandoval, S., Rodríguez, F., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111585 · Cited by 55

A carboxylic acid-functionalized coumarin-hemicyanine fluorescent dye and its application to construct a fluorescent probe for selective detection of cysteine over homocysteine and glutathione

Liu, J., Sun, Y., Zhang, H., Huo, Y., Shi, Y., Shi, H., & Guo, W. (2014) · RSC Advances · doi:10.1039/c4ra10865e · Cited by 54

Genes for iron–sulphur cluster assembly are targets of abiotic stress in rice, O ryza sativa

Liang, X., Qin, L., Liu, P., WANG, M., & Ye, H. (2013) · Plant Cell & Environment · doi:10.1111/pce.12198 · Cited by 53

Bacterial ApbC Can Bind and Effectively Transfer Iron−Sulfur Clusters

Boyd, J. M., Pierik, A. J., Netz, D. J. A., Lill, R., & Downs, D. M. (2008) · Biochemistry · doi:10.1021/bi800551y · Cited by 53

A coumarin-based fluorescent probe for thiols and its application in cell imaging

Liao, Y.-C., Venkatesan, P., Wei, L.-F., & Wu, S. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.04.027 · Cited by 52

Crucial Role of Conserved Cysteine Residues in the Assembly of Two Iron−Sulfur Clusters on the CIA Protein Nar1

Urzica, E. I., Pierik, A. J., Mühlenhoff, U., & Lill, R. (2009) · Biochemistry · doi:10.1021/bi900312x · Cited by 52

Cysteinome: The first comprehensive database for proteins with targetable cysteine and their covalent inhibitors

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New Targets and Inhibitors of Mycobacterial Sulfur Metabolism

Paritala, H., & Carroll, K. S. (2013) · Infectious Disorders - Drug Targets · doi:10.2174/18715265113139990022 · Cited by 51

Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis

Cai, K., Liu, G., Frederick, R. O., Xiao, R., Montelione, G. T., & Markley, J. L. (2016) · Structure · doi:10.1016/j.str.2016.08.020 · Cited by 54

Iron–Sulfur Cluster Biogenesis Systems and their Crosstalk

Xu, X. M., & Møller, S. G. (2008) · ChemBioChem · doi:10.1002/cbic.200800384 · Cited by 51

Synergistic effects of ion exchange and complexation processes in cysteine-modified clinoptilolite nanoparticles for removal of Cu( ii ) from aqueous solutions in batch and continuous flow systems

Fakari, S., & Nezamzadeh‐Ejhieh, A. (2017) · New Journal of Chemistry · doi:10.1039/c7nj00075h · Cited by 50

Solution Structure of the Iron−Sulfur Cluster Cochaperone HscB and Its Binding Surface for the Iron−Sulfur Assembly Scaffold Protein IscU

Füzéry, A. K., Tonelli, M., Ta, D. T., Cornilescu, G., Vickery, L. E., & Markley, J. L. (2008) · Biochemistry · doi:10.1021/bi800502r · Cited by 51

Alzheimer’s Disease and Parkinson’s Disease: A Review of Current Treatment Adopting a Nanotechnology Approach

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Overexpression of Drosophila mitoferrin in l(2)mbn cells results in dysregulation of Fer1HCH expression

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Long-term perturbation of muscle iron homeostasis following hindlimb suspension in old rats is associated with high levels of oxidative stress and impaired recovery from atrophy

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The Human Iron–Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules

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Evolution of mitochondrial protein biogenesis

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The functions of NifS-like proteins in plant sulfur and selenium metabolism

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Mitochondrial Proteomics in Experimental Autoimmune Uveitis Oxidative Stress

Saraswathy, S., & Rao, N. A. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2842 · Cited by 45

GTP Is Required for Iron-Sulfur Cluster Biogenesis in Mitochondria

Amutha, B., Gordon, D. M., Gu, Y., Lyver, E. R., Dancis, A., & Pain, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706808200 · Cited by 44

Metal and cofactor insertion

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Regulation and tissue-specific expression of δ-aminolevulinic acid synthases in non-syndromic sideroblastic anemias and porphyrias

Peoc’h, K., Nicolas, G., Schmitt, C., Mirmiran, A., Daher, R., Lefèbvre, T., Gouya, L., Karim, Z., & Puy, H. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.01.015 · Cited by 43

Targeting Bacterial Antioxidant Systems for Antibiotics Development

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Structural and Biochemical Characterization of Yeast Monothiol Glutaredoxin Grx6

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Gene atlas of iron‐containing proteins in Arabidopsis thaliana

Przybyla‐Toscano, J., Boussardon, C., Law, S. R., Rouhier, N., & Keech, O. (2021) · The Plant Journal · doi:10.1111/tpj.15154 · Cited by 45

Ancestral roles of eukaryotic frataxin: mitochondrial frataxin function and heterologous expression of hydrogenosomal Trichomonas homologues in trypanosomes

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Molecular chaperones involved in mitochondrial iron–sulfur protein biogenesis

Dutkiewicz, R., & Nowak, M. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1504-x · Cited by 41

Methods for Studying Iron Metabolism in Yeast Mitochondria

Molik, S., Lill, R., & Mühlenhoff, U. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80013-0 · Cited by 40

Escherichia coli FtnA acts as an iron buffer for re-assembly of iron–sulfur clusters in response to hydrogen peroxide stress

Bitoun, J. P., Wu, G., & Ding, H. (2008) · BioMetals · doi:10.1007/s10534-008-9154-7 · Cited by 39

Iron–Sulphur Clusters, Their Biosynthesis, and Biological Functions in Protozoan Parasites

Ali, V., & Nozaki, T. (2013) · Advances in Parasitology/Advances in parasitology · doi:10.1016/b978-0-12-407705-8.00001-x · Cited by 41

Impact of Sulfur on N2 Fixation of Legumes

Scherer, H. W. (2008) · Springer eBooks · doi:10.1007/978-3-540-76326-0_3 · Cited by 38

Identification of Vital and Dispensable Sulfur Utilization Factors in the Plasmodium Apicoplast

Haussig, J. M., Matuschewski, K., & Kooij, T. W. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089718 · Cited by 38

A fluorescence turn-on probe for cysteine and homocysteine based on thiol-triggered benzothiazolidine ring formation

Liu, S.-R., Chang, C.-Y., & Wu, S. (2014) · Analytica Chimica Acta · doi:10.1016/j.aca.2014.08.024 · Cited by 37

Tangled web of interactions among proteins involved in iron–sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies

Kim, J. H., Bothe, J. R., Alderson, T. R., & Markley, J. L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.020 · Cited by 38

Dual Localized AtHscB Involved in Iron Sulfur Protein Biogenesis in Arabidopsis

Xu, X. M., Lin, H., Latijnhouwers, M., & Møller, S. G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007662 · Cited by 37

Structural, mechanistic and coordination chemistry of relevance to the biosynthesis of iron–sulfur and related iron cofactors☆

Qi, W., & Cowan, J. A. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.10.016 · Cited by 37

Biogenic Metal Nanoparticles as A Potential Class of Antileishmanial Agents: Mechanisms and Molecular Targets

Ahmad, A., Ullah, S., Syed, F., Tahir, K., Khan, A. U., & Yuan, Q. (2020) · Nanomedicine · doi:10.2217/nnm-2019-0413 · Cited by 39

Blood Iron Homeostasis: Newly Discovered Proteins and Iron Imbalance

Bleackley, M. R., Wong, A. Y. K., Hudson, D. M., Wu, C., & MacGillivray, R. T. A. (2009) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2008.12.001 · Cited by 38

The competition between chemistry and biology in assembling iron–sulfur derivatives. Molecular structures and electrochemistry. Part II. {[Fe2S2](SγCys)4} proteins

Zanello, P. (2014) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2014.08.003 · Cited by 35

The endogenous adrenodoxin reductase-like flavoprotein arh1 supports heterologous cytochrome P450-dependent substrate conversions in Schizosaccharomyces pombe

Ewen, K. M., Schiffler, B., Uhlmann‐Schiffler, H., Bernhardt, R., & Hannemann, F. (2008) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2008.00360.x · Cited by 35

A highly selective fluorescent probe for Fe 3+ in living cells: a stress induced cell based model study

Sharma, N., Reja, S. I., Gupta, N., Bhalla, V., Kaur, D., Arora, S., & Kumar, M. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob02209j · Cited by 34

Mitochondrial [ 2Fe‐2S ] ferredoxins: new functions for old dogs

Schulz, V., Freibert, S., Boß, L., Mühlenhoff, U., Stehling, O., & Lill, R. (2022) · FEBS Letters · doi:10.1002/1873-3468.14546 · Cited by 34

The ABC-transporter AtmA is involved in nickel and cobalt resistance of Cupriavidus metallidurans strain CH34

Mikolay, A., & Nies, D. H. (2009) · Antonie van Leeuwenhoek · doi:10.1007/s10482-008-9303-6 · Cited by 34

Entamoeba histolytica mitosomes: Organelles in search of a function

Aguilera, P., Barry, T., & Tovar, J. (2007) · Experimental Parasitology · doi:10.1016/j.exppara.2007.08.004 · Cited by 34

Rapid and specific fluorescent probe visualizes dynamic correlation of Cys and HClO in OGD/R

Huang, P., Zhang, W., Wang, J., Huo, F., & Yin, C. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.109778 · Cited by 32

Reduction of Ethanol‐Derived Acetaldehyde Induced Motivational Properties by l ‐Cysteine

Peana, A. T., Assaretti, A., Muggironi, G., Enrico, P., & Diana, M. (2008) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2008.00809.x · Cited by 32

Disruption of the ATP-binding Cassette B7 (ABTM-1/ABCB7) Induces Oxidative Stress and Premature Cell Death in Caenorhabditis elegans

González‐Cabo, P., Bolinches-Amorós, A., Cabello, J., Ros, S., Moreno, S., Baylis, H. A., Palau, F., & Vázquez‐Manrique, R. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.211201 · Cited by 31

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Guo, Z., Xu, S., Chen, X., Wang, C., Yang, P., Qin, S., Zhao, C., Fei, F., Zhao, X., Tan, P., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-03344-2 · Cited by 31

Nutrient sulfur acquisition strategies employed by bacterial pathogens

Lensmire, J. M., & Hammer, N. D. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2018.11.002 · Cited by 30

The Staphylococcus aureus Cystine Transporters TcyABC and TcyP Facilitate Nutrient Sulfur Acquisition during Infection

Lensmire, J. M., Dodson, J. P., Hsueh, B. Y., Wischer, M. R., Delekta, P. C., Shook, J. C., Ottosen, E. N., Kies, P. J., Ravi, J., & Hammer, N. D. (2019) · Infection and Immunity · doi:10.1128/iai.00690-19 · Cited by 33

Transient iron coordination sites in proteins: Exploiting the dual nature of paramagnetic NMR

Piccioli, M., & Turano, P. (2014) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2014.05.007 · Cited by 30

Metabolism of Trichomonad Hydrogenosomes

Hrdý, I., Tachezy, J., & Müller, M. (2007) · Springer eBooks · doi:10.1007/7171_2007_110 · Cited by 30

Breeding of a Low Pyruvate-Producing Sake Yeast by Isolation of a Mutant Resistant to Ethyl α-Transcyanocinnamate, an Inhibitor of Mitochondrial Pyruvate Transport

Horie, K., Takahiro, O. B. A., Motomura, S., Isogai, A., Yoshimura, T., Tsuge, K., Koganemaru, K., Kobayashi, G., & Kitagaki, H. (2010) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.90373 · Cited by 29

The value of Arabidopsis research in understanding human disease states

Xu, X. M., & Møller, S. G. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.11.007 · Cited by 29

Fluorescent coumarin-based probe for cysteine and homocysteine with live cell application

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