Cited by 146Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsBiochemical Acid Research Studies

The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.

Aconitases: non-redox iron-sulfur proteins sensitive to reactive species

Castro, Laura, Tórtora, Verónica, Mansilla, Santiago, Radi, Rafael·2019·Accounts of Chemical Research

DOI 10.1021/acs.accounts.9b00150

Open this paper in CoChat — free account

Abstract

Conspectus Mammalian aconitases (mitochondrial and cytosolic isoenzymes) are unique iron–sulfur cluster-containing proteins in which the metallic center participates in the catalysis of a non-redox reaction. Within the cubane iron–sulfur cluster of aconitases only three of the four iron ions have cysteine thiolate ligands; the fourth iron ion (Fe α ) is solvent exposed within the active-site pocket and bound to oxygen atoms from either water or substrates to be dehydrated. The catalyzed reaction is the reversible isomerization of citrate to isocitrate with an intermediate metabolite, cis -aconitate. The cytosolic isoform of aconitase is a moonlighting enzyme; when intracellular iron is scarce, the complete disassembly of the iron–sulfur cluster occurs and apo-aconitase acquires the function of an iron responsive protein and regulates the translation of proteins involved in iron metabolism. In the late 1980s and during the 1990s, cumulative experimental evidence pointed out that aconitases are main targets of reactive oxygen and nitrogen species such as superoxide radical (O 2 •– ), hydrogen peroxide (H 2 O 2 ), nitric oxide ( • NO), and peroxynitrite (ONOO – ). These intermediates are capable of oxidizing the cluster, which leads to iron release and consequent loss of the catalytic activity of aconitase. As the reaction of the Fe–S cluster with O 2 •– is fast (∼10 7 M –1 s –1 ), quite specific, and reversible in vivo, quantification of active aconitase has been used to evaluate O 2 •– formation in cells. While • NO is modestly reactive with aconitase, its reaction with O 2 •– yields ONOO –, a strong oxidant that readily leads to the disruption of the Fe–S cluster. In the case of cytosolic aconitase, it has been seen that H 2 O 2 and • NO promote activation of iron responsive protein activity in cells. Proteomic advances in the 2000s confirmed that aconitases are main targets of reactive species in cellular models and in vivo, and other post-translational oxidative modifications such as protein nitration and carbonylation have been detected. Herein, we (1) outline the particular structural features of aconitase that make these proteins specific targets of reactive species, (2) characterize the reactions of O 2 •–, H 2 O 2, • NO, and ONOO – and related species with aconitases, (3) discuss how different oxidative post-translational modifications of aconitase impact the different functions of aconitases, and (4) argue how these proteins might function as redox sensors within different cellular compartments, regulating citrate concentration and efflux from mitochondria, iron availability in the cytosol, and cellular oxidant production.

Integrity signals

Registry

Crossref · 10.1021/acs.accounts.9b00150

Cites

70 of 70 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

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

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide.
Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., & Chaudhuri, G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.9265 · Cited by 5,074
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
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
Differential Inhibitory Action of Nitric Oxide and Peroxynitrite on Mitochondrial Electron Transport
Cassina, A., & Radí, R. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0178 · Cited by 721
Inhibition of Mitochondrial Electron Transport by Peroxynitrite
Radi, R., Rodriguez, M., Castro, L., & Telleri, R. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1013 · Cited by 693
Self-citation
Biochemistry of Peroxynitrite and Protein Tyrosine Nitration
Ferrer‐Sueta, G., Campolo, N., Trujillo, M., Bartesaghi, S., Carballal, S., Romero, N., Álvarez, B., & Radí, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00568 · Cited by 653
Peroxynitrite reactions and formation in mitochondria
Radí, R., Cassina, A., Hodara, R., Quijano, C., & Castro, L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01111-5 · Cited by 636
Self-citation
Oxidative damage during aging targets mitochondrial aconitase
Yan, L., Levine, R. L., & Sohal, R. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11168 · Cited by 620
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

Show all 70 references

Research works printed but not linked: 1

10.1042/bj3600209 · DOI

Sorted by citations

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335
Targeting oxidative stress in disease: Promise and limitations of antioxidant therapy
Forman, H. J., & Zhang, H. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00233-1 · Cited by 2,900
Mitochondrial dysfunction: mechanisms and advances in therapy
Yao, Z., Li, H., Liao, P., Chen, L., Pan, Y., Zheng, Y., Zhang, C., Liu, D., Zheng, M., & Gao, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01839-8 · Cited by 1,382
Regulation and function of the mammalian tricarboxylic acid cycle
Arnold, P. K., & Finley, L. W. S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102838 · Cited by 535
“This enzymatic requirement for iron makes ACO activity sensitive to iron levels within cells (150).”
Background
Mitochondrial iron–sulfur clusters: Structure, function, and an emerging role in vascular biology
Read, A. D., Bentley, R. E. T., Archer, S. L., & Dunham‐Snary, K. J. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102164 · Cited by 440
Superoxide Radicals in the Execution of Cell Death
Fujii, J., Homma, T., & Osaki, T. (2022) · Antioxidants · doi:10.3390/antiox11030501 · Cited by 337
Macrophage Polarization and Reprogramming in Acute Inflammation: A Redox Perspective
Pérez, S., & Rius-Pérez, S. (2022) · Antioxidants · doi:10.3390/antiox11071394 · Cited by 312
The Importance of Dietary Antioxidants on Oxidative Stress, Meat and Milk Production, and Their Preservative Aspects in Farm Animals: Antioxidant Action, Animal Health, and Product Quality—Invited Review
Ponnampalam, E. N., Kiani, A., Santhiravel, S., Holman, B. W. B., Lauridsen, C., & Dunshea, F. R. (2022) · Animals · doi:10.3390/ani12233279 · Cited by 325
Targeting Oxidative Stress and Inflammatory Response for Blood–Brain Barrier Protection in Intracerebral Hemorrhage
Chen, S., Li, L., Peng, C., Bian, C., Ocak, P. E., Zhang, J. H., Yang, Y., Zhou, D., Chen, G., & Luo, Y. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0072 · Cited by 197
Riding the tiger – physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix
Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123
Mitochondrial calcium and reactive oxygen species in cardiovascular disease
Murphy, E., & Liu, J. C. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac134 · Cited by 123
Role of oxidative stress in calcific aortic valve disease and its therapeutic implications
Greenberg, H. Z. E., Zhao, G., Shah, A. M., & Zhang, M. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab142 · Cited by 115
Targeting oxidative stress-mediated regulated cell death as a vulnerability in cancer
Chen, D., Guo, Z., Yao, L., Sun, Y., Dian, Y., Zhao, D., Ke, Y., Zeng, F., Zhang, C., Deng, G., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103686 · Cited by 95
Redox Activation of Mitochondrial DAMPs and the Metabolic Consequences for Development of Autoimmunity
Koenig, A., & Buskiewicz, I. A. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0073 · Cited by 78
Hypoxic-Ischemic Encephalopathy and Mitochondrial Dysfunction: Facts, Unknowns, and Challenges
Rodríguez-Rey, M., Valez, V., Cimarra, C., Blasina, F., & Radí, R. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8093 · Cited by 75
Nitric oxide regulation of cellular metabolism: Adaptive tuning of cellular energy
Pappas, G., Wilkinson, M. L., & Gow, A. J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.11.006 · Cited by 74
Regulation of Keap1-Nrf2 signaling in health and diseases
Xiao, J.-L., Liu, H.-Y., Sun, C., & Tang, C. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09771-4 · Cited by 73
Oxidative Metabolism as a Cause of Lipid Peroxidation in the Execution of Ferroptosis
Fujii, J., & Imai, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147544 · Cited by 65
Iron–sulfur clusters as inhibitors and catalysts of viral replication
Ebrahimi, K. H., Ciofi‐Baffoni, S., Hagedoorn, P., Nicolet, Y., Brun, N. E. L., Hagen, W. R., & Armstrong, F. A. (2022) · Nature Chemistry · doi:10.1038/s41557-021-00882-0 · Cited by 63
The glyco-redox interplay: Principles and consequences on the role of reactive oxygen species during protein glycosylation
Khoder‐Agha, F., & Kietzmann, T. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101888 · Cited by 56
Redox proteomics combined with proximity labeling enables monitoring of localized cysteine oxidation in cells
Kisty, E. A., Falco, J. A., & Weerapana, E. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.006 · Cited by 55
Mitochondrial NAD(P) + Transhydrogenase: From Molecular Features to Physiology and Disease
Francisco, A., Figueira, T. R., & Castilho, R. F. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0111 · Cited by 51
An ESIPT-based fluorescent probe with fast-response for detection of hydrogen sulfide in mitochondria
Du, Y., Wang, H., Zhang, T., Wen, W., Li, Z., Bi, M., & Liu, J. (2021) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2021.120390 · Cited by 45
Free radicals and oxidative stress: Mechanisms and therapeutic targets
Hassan, H. A., Ahmed, H. S., & Hassan, D. F. (2024) · Human Antibodies · doi:10.3233/hab-240011 · Cited by 51
Involvement of Nitric Oxide in Protecting against Radical Species and Autoregulation of M1-Polarized Macrophages through Metabolic Remodeling
Fujii, J., & Osaki, T. (2023) · Molecules · doi:10.3390/molecules28020814 · Cited by 42
Middle age as a turning point in mouse cerebral cortex energy and redox metabolism: Modulation by every-other-day fasting
Bayliak, M. M., Sorochynska, O. M., Kuzniak, O. V., Gospodaryov, D. V., Demianchuk, O., Vasylyk, Y. V., Mosiichuk, N. M., Storey, K. B., Garaschuk, O., & Lushchak, V. I. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111182 · Cited by 39
Ketogenesis controls mitochondrial gene expression and rescues mitochondrial bioenergetics after cervical spinal cord injury in rats
Seira, O., Kolehmainen, K., Liu, J., Streijger, F., Haegert, A. M., LeBihan, S., Boushel, R., & Tetzlaff, W. (2021) · Scientific Reports · doi:10.1038/s41598-021-96003-5 · Cited by 38
Activation of ALDH1A1 by omeprazole reduces cell oxidative stress damage
Calleja, L. F., Yoval‐Sánchez, B., Hernández‐Esquivel, L., Gallardo‐Pérez, J. C., Sosa‐Garrocho, M., Marín‐Hernández, Á., Jasso‐Chávez, R., Macías‐Silva, M., & Rodríguez‐Zavala, J. S. (2021) · FEBS Journal · doi:10.1111/febs.15698 · Cited by 36
An Artificial [Fe4S4]-Containing Metalloenzyme for the Reduction of CO2 to Hydrocarbons
Waser, V., Mukherjee, M., Tachibana, R., Igareta, N. V., & Ward, T. R. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c03546 · Cited by 34
A mitochondria-targeted single fluorescence probe for separately and continuously visualizing H2S and Cys with multi-response signals
Zhao, X., Ji, H., Hasrat, K., Misal, S., He, F., Dai, Y., Ma, F., & Qi, Z. (2020) · Analytica Chimica Acta · doi:10.1016/j.aca.2020.02.017 · Cited by 34
Nutritional strategies to reduce intestinal cell apoptosis by alleviating oxidative stress
Li, B., Zhang, X., Zhang, Q., Zheng, T., Li, Q., Yang, S., Shao, J., Guan, W., & Zhang, S. (2024) · Nutrition Reviews · doi:10.1093/nutrit/nuae023 · Cited by 29
Redox sensitive human mitochondrial aconitase and its interaction with frataxin: In vitro and in silico studies confirm that it takes two to tango
Mansilla, S., Tórtora, V., Pignataro, M. F., Sastre, S., Castro, I. H., Chiribao, M. L., Robello, C., Zeida, A., Santos, J., & Castro, L. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.01.028 · Cited by 27
Self-citation
A defect in mitochondrial fatty acid synthesis impairs iron metabolism and causes elevated ceramide levels
Dutta, D., Kanca, O., Byeon, S. K., Marcogliese, P. C., Zuo, Z., Shridharan, R. V., Park, J. H., Undiagnosed Diseases Network, Lin, G., Ge, M. J., et al. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00873-0 · Cited by 26
Impaired Iron–Sulfur Cluster Synthesis Induces Mitochondrial PARthanatos in Diabetic Cardiomyopathy
Wang, M., Zhang, S., Tian, J., Yang, F., Chen, H., Bai, S., Kang, J., Pang, K., Huang, J., Dong, M., et al. (2024) · Advanced Science · doi:10.1002/advs.202406695 · Cited by 25
Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View
Nicolet, Y., Cherrier, M. V., & Amara, P. (2021) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.1c00044 · Cited by 22
Redox-Regulated Iron Metabolism and Ferroptosis in Ovarian Cancer: Molecular Insights and Therapeutic Opportunities
Liu, D., Hu, Z., Lu, J., & Yi, C. (2024) · Antioxidants · doi:10.3390/antiox13070791 · Cited by 22
Staphylococcal aconitase expression during iron deficiency is controlled by an sRNA-driven feedforward loop and moonlighting activity
Barrault, M., Chabelskaya, S., Coronel-Tellez, R. H., Toffano-Nioche, C., Jacquet, E., & Bouloc, P. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae506 · Cited by 20
Mitochondrial ribosome biogenesis and redox sensing
Brischigliaro, M., Sierra‐Magro, A., Ahn, A., & Barrientos, A. (2024) · FEBS Open Bio · doi:10.1002/2211-5463.13844 · Cited by 20
Determination of the Absolute Molar Mass of [Fe-S]-Containing Proteins Using Size Exclusion Chromatography-Multi-Angle Light Scattering (SEC-MALS)
Velours, C., Zhou, J., Zecchin, P., He, N., Salameh, M., Golinelli‐Cohen, M., & Golinelli‐Pimpaneau, B. (2022) · Biomolecules · doi:10.3390/biom12020270 · Cited by 20
Three enzymes governed the rise of O2 on Earth
Mrnjavac, N., Degli Esposti, M., Mizrahi, I., Martin, W. F., & Allen, J. F. (2024) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2024.149495 · Cited by 18
Oxidative stress and programmed cell death in diabetic wounds: A comprehensive review
Hong, L., Li, M., & Fan, Y. (2025) · Science Progress · doi:10.1177/00368504251370676 · Cited by 22
Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology
Huang, X., Harmer, J. R., Schenk, G., & Southam, G. (2024) · Frontiers in Chemistry · doi:10.3389/fchem.2024.1349020 · Cited by 18
Defenses of multidrug resistant pathogens against reactive nitrogen species produced in infected hosts
Carvalho, S. M., Beas, J. Z., Videira, M. A. M., & Saraiva, L. M. (2022) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2022.02.001 · Cited by 15
Prediction of the Iron–Sulfur Binding Sites in Proteins Using the Highly Accurate Three-Dimensional Models Calculated by AlphaFold and RoseTTAFold
Golinelli‐Pimpaneau, B. (2021) · Inorganics · doi:10.3390/inorganics10010002 · Cited by 16
Unveiling the role of inorganic nanoparticles in Earth’s biochemical evolution through electron transfer dynamics
Huang, X. (2024) · iScience · doi:10.1016/j.isci.2024.109555 · Cited by 16
Binding of α-synuclein to ACO2 promotes progressive mitochondrial dysfunction in Parkinson's disease models
Jiao, J., Gao, G., Zhu, J., Wang, C., Liu, L., & Yang, H. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103399 · Cited by 15
Aqueous stability and redox chemistry of synthetic [Fe4S4] clusters
Waser, V., & Ward, T. R. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215377 · Cited by 13
Redox remodeling of central metabolism as a driving force for cellular protection, proliferation, differentiation, and dysfunction
Fujii, J. (2024) · Free Radical Research · doi:10.1080/10715762.2024.2407147 · Cited by 13
The Key Enzymes of Carbon Metabolism and the Glutathione Antioxidant System Protect Yarrowia lipolytica Yeast Against pH-Induced Stress
Rakhmanova, T. I., Гесслер, Н. Н., Isakova, E. P., Klein, O. I., Deryabina, Y. I., & Попова, Т. Н. (2024) · Journal of Fungi · doi:10.3390/jof10110747 · Cited by 13
Monoamine oxidase mediated oxidative stress: a potential molecular and biochemical crux in the pathogenesis of obesity
Niveta, J. P. S., John, C. M., & Arockiasamy, S. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08938-9 · Cited by 12
Singlet oxygen-induced signalling depends on the metabolic status of the Chlamydomonas reinhardtii cell
Youssef, W. A., Feil, R., Saint‐Sorny, M., Johnson, X., Lunn, J. E., Grimm, B., & Brzezowski, P. (2023) · Communications Biology · doi:10.1038/s42003-023-04872-5 · Cited by 12
The importance of aquaporin-8 for cytokine-mediated toxicity in rat insulin-producing cells
Krüger, C., Jörns, A., Kaynert, J. T., Waldeck‐Weiermair, M., Michel, T. M., Elsner, M., & Lenzen, S. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.08.003 · Cited by 12
Studying Acetylation of Aconitase Isozymes by Genetic Code Expansion
Araujo, J., Ottinger, S., Venkat, S., Gan, Q., & Fan, C. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.862483 · Cited by 12
Molecular pathways of generation and detoxification of reactive oxygen species and induction of apoptosis in yeasts
Gull, S., Shabbir, C. A., Khan, Z., Bukhari, D. A., & Rehman, A. (2024) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2024.106069 · Cited by 10
Perturbed Brain Glucose Metabolism Caused by Absent SIRT3 Activity
Kristián, T., Karimi, A. J., Fearnow, A. D., Waddell, J., & McKenna, M. C. (2021) · Cells · doi:10.3390/cells10092348 · Cited by 10
Proteomic strategies to interrogate the Fe-S proteome
Bak, D. W., & Weerapana, E. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119791 · Cited by 10
Metabolic Responses to Redox Stress in Vascular Cells
Xiao, W., Lee, L. Y.-H., & Loscalzo, J. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0476 · Cited by 9
Potential Role of Oxidative Stress in the Pathophysiology of Neurodegenerative Disorders
Singh, S. K., Ahuja, A., & Pathak, S. (2024) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/0113862073280680240101065732 · Cited by 10
New perspectives on the role of biological factors in anorexia nervosa: Brain volume reduction or oxidative stress, which came first?
Gaiaschi, L., Priori, E. C., Mensi, M. M., Verri, M., Buonocore, D., Parisi, S., Hernandez, L. N. Q., Brambilla, I., Ferrari, B., Luca, F. D., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106580 · Cited by 9
Mitochondrial De Novo Assembly of Iron–Sulfur Clusters in Mammals: Complex Matters in a Complex That Matters
Perfitt, T. L., & Martelli, A. (2022) · Inorganics · doi:10.3390/inorganics10030031 · Cited by 8
Medication targeting to subcellular organelles: Emphasizing mitochondria as a therapeutic marvel—Current situation and future prospects
Alzhrani, R. F., Alhowyan, A., Taha, E. I., Attia, S. M., Salama, S. A., & Harisa, G. I. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114647 · Cited by 7
Hydroxylamine promotes partial nitrification by selectively inhibiting Comammox and NOB: activity partitioning and metaproteomic evidence
Shi, L., Min, W., Liu, J., Bu, Y., Wei, Y., & Ma, B. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.169583 · Cited by 7
Assessing metal ion transporting activity of ZIPs: Intracellular zinc and iron detection
Xiao, G., Li, H., Zhao, M., & Zhou, B. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.05.011 · Cited by 7
Differential manifestation of RONS and antioxidant enzymes in response to singular versus combinatorial stress in Chironomus ramosus
Bomble, P., & Nath, B. B. (2022) · Stress Biology · doi:10.1007/s44154-022-00077-8 · Cited by 7
Studying lysine acetylation of citric acid cycle enzymes by genetic code expansion
Fatema, N., & Fan, C. (2023) · Molecular Microbiology · doi:10.1111/mmi.15052 · Cited by 6
Mapping of oxidative modifications on the alpha-keto glutarate dehydrogenase complex induced by singlet oxygen: Effects on structure and activity
Gao, Q., Hägglund, P., Gamon, L. F., & Davies, M. J. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.09.024 · Cited by 5
Implications for soluble iron accumulation, oxidative stress, and glial glutamate release in motor neuron death associated with sporadic amyotrophic lateral sclerosis
Shibata, N., Kataoka, I., Okamura, Y., Murakami, K., Kato, Y., Yamamoto, T., & Masui, K. (2025) · Neuropathology · doi:10.1111/neup.13033 · Cited by 7
A [4Fe-4S] cluster resides at the active center of phosphomevalonate dehydratase, a key enzyme in the archaeal modified mevalonate pathway
Komeyama, M., Kanno, K., Mino, H., Yasuno, Y., Shinada, T., Ito, T., & Hemmi, H. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1150353 · Cited by 6
Photoinduced NO release of [Fe 2 (μ-SL) 2 (NO) 4 ] complexes and their protein adducts: insights from structure, cytotoxicity, and photodynamic studies
Gong, W., Pang, Y., Wang, C., Wang, W., & Wang, H. (2025) · Inorganic Chemistry Frontiers · doi:10.1039/d5qi00255a · Cited by 5
Hierarchically assembled curcumin-vitamin E-zinc thermo-gel for multi-synergistic prevention and treatment of radiation-induced oral mucositis
Duan, J., Chen, M., Wang, M., He, R., Li, K., & Shi, L. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102525 · Cited by 5
Aspergillus fumigatus cytochrome c impacts conidial survival during sterilizing immunity
James, M. R., Aufiero, M. A., Vesely, E. M., Dhingra, S., Liu, K.-W., Hohl, T. M., & Cramer, R. A. (2023) · mSphere · doi:10.1128/msphere.00305-23 · Cited by 5
CISD2-mediated mitochondrial dysfunction and iron redistribution contributes to ferroptosis in arsenic-induced nonalcoholic steatohepatitis
Zhang, J., Wang, L., Yang, L., Zheng, F., Ding, X., Yao, X., Bai, J., Wang, N., Yang, G., Qiu, T., et al. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.117694 · Cited by 5
Anticancer activity promoted by ligand diversity in diiron thiocarbyne complexes
Mihajlović, E., Biancalana, L., Mojić, M., Jelača, S., Chiaverini, L., Zacchini, S., Mijatović, S., Maksimović‐Ivanić, D., & Marchetti, F. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117364 · Cited by 5
A classification scheme for inorganic cluster compounds based on their electronic structures and bonding characteristics
Lin, Z. (2024) · Chinese Journal of Structural Chemistry · doi:10.1016/j.cjsc.2024.100254 · Cited by 5
Association Between Serum Uric Acid Levels and Metabolic-Associated Fatty Liver Disease in Southeast China: A Cross-Sectional Study
Ren, S., Chen, S., Huang, J., Yu, R., Wu, Y., & Peng, X. (2024) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s476045 · Cited by 5
Low magnetic fields stimulate cardiac mitochondrial bioenergetics with a bell-shaped response: Possibly via a radical pair mechanism
Beutner, G., Yuh, H.-J., Goldenberg, I., Wallace, D. C., Porter, G. A., Jr., Moss, A. J., & Sheu, S. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.11.055 · Cited by 5
Long-term facilitation of catecholamine secretion from adrenal chromaffin cells of neonatal rats by chronic intermittent hypoxia
Makarenko, V. V., Peng, Y., Khan, S. A., Nanduri, J., Fox, A. P., & Prabhakar, N. R. (2019) · Journal of Neurophysiology · doi:10.1152/jn.00435.2019 · Cited by 5
Unravelling Mechanisms of Oxinflammation Induced by Heavy Metals
Guimarães‐Ervilha, L. O., Assis, M. Q., Lopes, I. D. S., Iasbik‐Lima, T., Faria, J. J. S., Souza, A. C. F., & Machado‐Neves, M. (2026) · Metabolites · doi:10.3390/metabo16050319 · Cited by 4
Investigating Iron-Sulfur Proteins in Infectious Diseases: A Review of Characterization Techniques
Raza, M. K., Jeyachandran, V. R., & Bashir, S. (2024) · Inorganics · doi:10.3390/inorganics12010025 · Cited by 4
Disruption of sulfur transferase complex increases bacterial intramacrophage persistence
Tang, H., Wang, Z., Li, C., Yu, J., Huang, W., Zhou, T., Zhang, C., Wen, B., Wang, C., Zhu, X., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013136 · Cited by 4
CYBB as a potential therapeutic target through influencing ferroptosis and macrophage in ovarian cancer
Tian, Y., Wu, S. F., & Wang, X. Y. (2025) · Discover Oncology · doi:10.1007/s12672-025-02891-8 · Cited by 4
When Pathways Converge: Iron, Lipid Peroxidation, and α‐Synuclein in Ferroptosis‐Driven Dopaminergic Neurodegeneration
Sperlich, C. L., Stockwell, B. R., & Farina, M. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70438 · Cited by 5
Electromagnetic fields regulate iron metabolism: From mechanisms to applications
Wang, S., Yang, J., Zhen, C., Wang, H., & Shang, P. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.04.044 · Cited by 4
Galectin-3 S-glutathionylation regulates its effect on adipocyte insulin signaling
Maurya, M., Jaiswal, A., Gupta, S., Ali, W., Gaikwad, A. N., Dikshit, M., & Barthwal, M. K. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119234 · Cited by 4
Kinetic and Regulatory Properties of Yarrowia lipolytica Aconitate Hydratase as a Model-Indicator of Cell Redox State under pH Stress
Rakhmanova, T. I., Sekova, V. Y., Gessler, N. N., Isakova, E. P., Deryabina, Y. I., Попова, Т. Н., Shurubor, Y. I., & Krasnikov, B. F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087670 · Cited by 4
Hyperuricemia in Chinese Patients with Mood Disorders: Prevalence, Related Factors, and Predictive Model
Wang, X., Wang, S., Qi, W., Wang, Y., Zhang, L., & Sun, P. (2025) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s535310 · Cited by 3
The Secretome of Adult Murine Hookworms Is Shaped by Host Expression of STAT6
Ferguson, A. A., Rossi, H. L., & Herbert, D. R. (2024) · Parasite Immunology · doi:10.1111/pim.13056 · Cited by 3
Ascorbic acid deficiency promotes metabolic remodeling and pulmonary fibrosis that leads to respiratory failure in Sod1 and Akr1a double-knockout mice
Osaki, T., Homma, T., Soma, Y., Miyata, S., Matsuda, Y., & Fujii, J. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103749 · Cited by 3
Isolation and characterization of bacteriocin-like substances from Bacillus paranthracis strain MHSD3, a potential probioticPreprint
Diale-Makhongela, M. O., Abrahams, A. M., & Serepa‐Dlamini, M. H. (2022) · Research Square · doi:10.21203/rs.3.rs-1553916/v1 · Cited by 3
On the occurrence of a glutaredoxin-like small protein in the anaerobic protozoan parasite Entamoeba histolytica
Birocco, F., Gonzalez, L. N., Guerrero, S. A., Iglesias, A. Á., & Arias, D. G. (2023) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2023.130489 · Cited by 2
The iron metalloproteome of Pseudomonas aeruginosa under oxic and anoxic conditions
Saito, M. A., & McIlvin, M. R. (2025) · Metallomics · doi:10.1093/mtomcs/mfaf023 · Cited by 3
Direct CO 2 Reduction to CO with an Fe 4 S 4 -Based Coordination Polymer
Le, L., Darù, A., Kunstelj, Š., Wuttig, A., Gagliardi, L., & Anderson, J. R. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c23180 · Cited by 2
PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote erythropoiesis and megakaryopoiesis
Liu, G., Hou, Y., Jin, X., Zhang, Y., Sun, C., Huang, C., Ren, Y., Gao, J., Wang, X., & Jiang, X. (2024) · eLife · doi:10.7554/elife.95815 · Cited by 2
PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote erythropoiesis and megakaryopoiesis
Liu, G., Hou, Y., Jin, X., Zhang, Y., Sun, C., Huang, C., Ren, Y., Gao, J., Wang, X., & Jiang, X. (2024) · eLife · doi:10.7554/elife.95815.3 · Cited by 2
Insight into the photodynamic mechanism and protein binding of a nitrosyl iron−sulfur [Fe2S2(NO)4]2− cluster
Gong, W., Wu, T., Liu, Y., Jiao, S., Wang, W., Yan, W., Li, Y., Liu, Y., Zhang, Y., & Wang, H. (2024) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2024.124603 · Cited by 2
Functionalization of Mesoporous Silica with a G-A-Mismatched dsDNA Chain for Efficient Identification and Selective Capturing of the MutY Protein
Sun, J., Wang, J., & Chen, X. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c19257 · Cited by 2
Branched-chain amino acid catabolism depends on GRXS15 through mitochondrial lipoyl cofactor homeostasisPreprint
Moseler, A., Kruse, I., Maclean, A. E., Pedroletti, L., Wagner, S., Wehler, R., Fischer-Schrader, K., Poschet, G., Wirtz, M., Dörmann, P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.13.947697 · Cited by 2
TtuA and TudS, Two [4Fe‐4S]‐Dependent Enzymes Catalyzing Nonredox Sulfuration or Desulfuration Reactions
Zhou, J., Bimaï, O., Arragain, S., Pecqueur, L., & Golinelli‐Pimpaneau, B. (2022) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2811 · Cited by 2
Mechanism Action of Iron Regulatory Protein 1 (IRP1/ACO1) in Disease
闫, 妠. (2022) · Advances in Clinical Medicine · doi:10.12677/acm.2022.12121680 · Cited by 1
Can iron chelators ameliorate viral infections?
Pereira, T. A., & Espósito, B. P. (2023) · BioMetals · doi:10.1007/s10534-023-00558-x · Cited by 1

Authors: Castro, L., Tórtora, V., Mansilla, S., & Radi, R.
Affiliations: Universidad de la República de Uruguay (UY)
Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Av. General Flores 2125, 11800 Montevideo, Uruguay
Corresponding author: Castro, Laura
ORCID: Castro, Laura
Mansilla, Santiago
Radi, Rafael
Venue: Accounts of Chemical Research
Publisher: American Chemical Society (ACS)
Published: 2019-07-09
Volume: 52
Issue: 9
Pages: 2609-2619
ISSN: 0001-4842 (ISSN-L)
1520-4898
DOI: 10.1021/acs.accounts.9b00150
OpenAlex: W2959204530
Cited by: 146
References: 70
Citations by year: 2026: 18 · 2025: 27 · 2024: 33 · 2023: 22 · 2022: 20 · 2021: 19 · 2020: 6 · 2019: 1
FWCI: 2.45
Type: journal article
Language: en
Open access: closed
Licence: doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-045 (stm-asf)
Locations: Accounts of Chemical Research (publishedVersion)
PubMed (publishedVersion)
Funders: Universidad de la Rep?blica Uruguay (EI 2015)
Comisi?n Sectorial de Investigaci?n Cient?fica (I+D 2016)
Fundaci?n Manuel Perez
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
Keywords: aconitase, iron-sulfur clusters, reactive oxygen species, reactive nitrogen species, superoxide, peroxynitrite, hydrogen peroxide, nitric oxide, iron metabolism, cis-aconitate, protein nitration, protein carbonylation, iron deficiency, mitochondrial aconitase
MeSH terms: Aconitate Hydratase, Animals, Humans, Hydrogen Peroxide, Mitochondria, Models, Molecular, Nitric Oxide, Superoxides, Peroxynitrous Acid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Aconitases: non-redox iron-sulfur proteins sensitive to reactive species

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks