Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAconitase as Iron−Sulfur Protein, Enzyme, and Iron-Regulatory ProteinHelmut Beinert, Mary Claire Kennedy, and C. David StoutView Author Information Institute for Enzyme Research, Graduate School, and Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53705, Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037 Cite this: Chem. Rev. 1996, 96, 7, 2335–2374Publication Date (Web):November 7, 1996Publication History Received21 February 1996Revised20 May 1996Published online7 November 1996Published inissue 1 January 1996https://pubs.acs.org/doi/10.1021/cr950040zhttps://doi.org/10.1021/cr950040zresearch-articleACS PublicationsCopyright © 1996 American Chemical SocietyRequest reuse permissionsArticle Views4873Altmetric-Citations499LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Cluster chemistry,Iron-sulfur clusters,Monomers,Peptides and proteins,Surface interactions Get e-Alerts
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Mitochondrial aconitase is a ferrosulphoprotein in the mitochondrial matrix that catalyses reversible isomerisation of citrate to isocitrate via cis-aconitate in the Krebs cycle.
“Mitochondrial aconitase is a ferrosulphoprotein located in the mitochondrial matrix that catalyses the reversible isomerisation of citrate to isocitrate via cis-aconitate in the Krebs cycle [111], Figure 44.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [111]
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Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
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“It contains a cubane-type [4Fe-4S] center with three iron atoms interacting with cysteine residues and inorganic sulfur atoms, while the fourth iron, Fe- , is exposed to the solvent that allows the catalytic dehydration of citrate to form the intermediate cis-aconitate, as well as the subsequent hydration of cis-aconi…”
BackgroundIron-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
Self-citationStructure, function, and formation of biological iron-sulfur clusters
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The role of iron regulatory proteins in mammalian iron homeostasis and disease
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“In aconitases, a cubane iron-sulfur cluster is ligated by three cysteines within the enzymatic active site cleft, and the fourth iron of the cubane cluster binds substrat”
BackgroundStructural Basis of Biological Nitrogen Fixation
Howard, J. B., & Rees, D. C. (1996) · Chemical Reviews · doi:10.1021/cr9500545 · Cited by 1,060 · see citing works
RadicalS-Adenosylmethionine Enzymes
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Hypoxia and Metabolic Adaptation of Cancer Cells
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I RON R EGULATORY P ROTEINS AND THE M OLECULAR C ONTROL OF M AMMALIAN I RON M ETABOLISM
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Synthetic Analogues of the Active Sites of Iron−Sulfur Proteins
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Nitric oxide and iron proteins
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“IRPs differ from one another in that IRE-binding activity of IRP1 is regulated primarily by reversible binding of a labile iron-sulfur cluste”
BackgroundMammalian 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
“However, aconitases have long been known to sense ROS and RNS because their [4Fe – 4S] cluster is solvent accessible and these reactive species can initiate cluster loss (reviewed in [65]).”
BackgroundSynthetic Analogues and Reaction Systems Relevant to the Molybdenum and Tungsten Oxotransferases
Enemark, J. H., Cooney, J. J. A., Wang, J., & Holm, R. H. (2003) · Chemical Reviews · doi:10.1021/cr020609d · Cited by 472 · see citing works
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Green, J. D., & Paget, M. S. B. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1022 · Cited by 412 · see citing works
Modulation of Mitochondrial Function by Hydrogen Peroxide
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Metal Ion Modeling Using Classical Mechanics
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Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity
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Self-citationThe role of Fe–S proteins in sensing and regulation in bacteria
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Self-citationMethylerythritol Phosphate Pathway of Isoprenoid Biosynthesis
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“Coordination of the C3-OH group of MEcPP (16) to the [4Fe-4S] cluster may also facilitate the 30 → 31 transformation, as in the case of aconitase (72).”
Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster
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“As, at the time of these experiments, such conversions had rarely been observed with proteins [23,27], independent con¢rmation was sought by Moëssbauer spectroscopy.”
MethodSelf-citationNon-Heme Iron Nitrosyls in Biology
Butler, A. R., & Megson, I. L. (2002) · Chemical Reviews · doi:10.1021/cr000076d · Cited by 343 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
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Mitochondrial Aconitase Is a Source of Hydroxyl Radical
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Self-citationDoxorubicin induced heart failure: Phenotype and molecular mechanisms
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Nitric Oxide and Peroxynitrite Interactions with Mitochondria
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“dant-sensitive site due to the labile nature of its 4Fe-4S cluster, which readily evolves to 3Fe-4S upon the reaction with various oxidants (Beinert et al., 1996).”
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287 · see citing works
“Aconitases are ancient enzymes that interconvert citrate to isocitrate through a stereospecific dehydration/rehydration mechanism requiring direct binding of substrate to the [4Fe–4S] cluster [96,97].”
BackgroundIron–sulfur proteins with nonredox functions
Flint, D. H., & Allen, R. M. (1996) · Chemical Reviews · doi:10.1021/cr950041r · Cited by 280 · see citing works
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Self-citationMammalian Tissue Oxygen Levels Modulate Iron-Regulatory Protein Activities in Vivo
Meyron‐Holtz, E. G., Ghosh, M. C., & Rouault, T. A. (2004) · Science · doi:10.1126/science.1103786 · Cited by 246 · see citing works
Structural Basis for the Mechanism of Respiratory Complex I
Berrisford, J. M., & Sazanov, L. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032144 · Cited by 247 · see citing works
Developments in the Biomimetic Chemistry of Cubane-Type and Higher Nuclearity Iron–Sulfur Clusters
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Iron regulatory proteins and their role in controlling iron metabolism
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Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria
Bulteau, A.-L., Ikeda-Saito, M., & Szweda, L. I. (2003) · Biochemistry · doi:10.1021/bi0353979 · Cited by 241 · see citing works
How many metals does it take to fix N 2 ? A mechanistic overview of biological nitrogen fixation
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Density Functional and Reduction Potential Calculations of Fe 4 S 4 Clusters
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The Interface Between the Biological and Inorganic Worlds: Iron-Sulfur Metalloclusters
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S-Adenosylmethionine: A Wolf in Sheep's Clothing, or a Rich Man's Adenosylcobalamin?
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Contrasting Sensitivities of Escherichia coli Aconitases A and B to Oxidation and Iron Depletion
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Iron—sulfur proteins: new roles for old clusters
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Fe-S proteins in sensing and regulatory functions
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Self-citationX-ray crystal structure of the light-independent protochlorophyllide reductase
Muraki, N., Nomata, J., Ebata, K., Mizoguchi, T., Shiba, T., Tamiaki, H., Kurisu, G., & Fujita, Y. (2010) · Nature · doi:10.1038/nature08950 · Cited by 201 · see citing works
FeMo Cofactor of Nitrogenase: A Density Functional Study of States MN, MOX, MR, and MI
Lovell, T., Li, J., Liu, T., Case, D. A., & Noodleman, L. (2001) · Journal of the American Chemical Society · doi:10.1021/ja011860y · Cited by 195 · see citing works
Selectivity of protein oxidative damage during aging in Drosophila melanogaster
Nilanjana, D. A. S., Levine, R. L., Orr, W. C., & Sohal, R. S. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600209 · Cited by 186 · see citing works
Oxidation of thiol compounds by molecular oxygen in aqueous solutions
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The Structure and Function of Frataxin
Bencze, K. Z., Kondapalli, K. C., Cook, J. D., McMahon, S., Millán‐Pacheco, C., Pastor, N., & Stemmler, T. L. (2006) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230600846058 · Cited by 164 · see citing works
“Damage to aconitase, a Krebs-cycle enzyme that converts citrate to isocitrate (Beinert et al., 1996), has shown to be a marker for cellular oxidative damage (Bulteau et al., 2003).”
BackgroundModel-based metabolic engineering enables high yield itaconic acid production by Escherichia coli
Harder, B., Bettenbrock, K., & Klamt, S. (2016) · Metabolic Engineering · doi:10.1016/j.ymben.2016.05.008 · Cited by 163 · see citing works
Structural Conversions of Synthetic and Protein-Bound Iron–Sulfur Clusters
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Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis
Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 158 · see citing works
“The citric acid cycle enzyme aconitase contains a [4Fe–4S] clus- ter and the enzymatic reaction catalyzed by aconitase involves substrate coordination to a specific iron atom in this cluster (Beinert et al. 1996).”
BackgroundHänzelmann, P., & Schindelin, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510711103 · Cited by 158 · see citing works
Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
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“They are monomeric enzymes containing single iron–sulphur clusters which are interconvertible between the catalytically active [4Fe–4S] forms and the inactive [3Fe–4S] and apo-enzyme forms (Beinert et al., 1996).”
BackgroundProteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae
Tsvetanova, N. G., Klass, D. M., Salzman, J., & Brown, P. O. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012671 · Cited by 153 · see citing works
“In support of this hypothesis, aconitase, originally annotated as an enzyme with a central role in energy production, was later discovered to play a role in post-transcriptional regulation of iron metabolism through interaction with an RNA stem-loop aptamer [40,41].”
BackgroundThe α-Aminoadipate Pathway for Lysine Biosynthesis in Fungi
Xu, H., Andi, B., Qian, J., et al. (2006) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:46:1:43 · Cited by 157 · see citing works
“However, little is known of the mechanism of the homoaconitase, but its mechanism may be similar to that of aconitase ( 82 ).”
BackgroundHänzelmann, P., Hernández, H. L., Menzel, C., García‐Serres, R., Huynh, B. H., Johnson, M. K., Mendel, R. R., & Schindelin, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313398200 · Cited by 153 · see citing works
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Outlining the Complex Pathway of Mammalian Fe-S Cluster Biogenesis
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“Besides their involvement in redox reactions, Fe-S enzymes are known to have essential roles in several metabolic pathways, with one of the most notable examples being mitochondrial aconitase of the tricarboxylic acid cycle (TCA) cycle, which ligates a solventexposed [4Fe-4S] cluster that directly participates in subs…”
BackgroundKülzer, R., Pils, T., Kappl, R., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.4897 · Cited by 149 · see citing works
Aconitases: non-redox iron-sulfur proteins sensitive to reactive species
Castro, L., Tórtora, V., Mansilla, S., & Radi, R. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.9b00150 · Cited by 146 · see citing works
Beinert, H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01637.x · Cited by 159 · see citing works
“and MoÈssbauer spectroscopy and crystal structures [21,63].”
Self-citationCrystal Structure of Human Iron Regulatory Protein 1 as Cytosolic Aconitase
Dupuy, J., Volbeda, A., Carpentier, P., Darnault, C., Moulis, J., & Fontecilla-Camps, J. C. (2006) · Structure · doi:10.1016/j.str.2005.09.009 · Cited by 145 · see citing works
“Moreover, S778 of IRP1, which in mAcn is proposed to provide an alkoxyde that removes the Ca proton during dehydration of the citrate substrate (Beinert et al., 1996) (see also Figure 3), is substituted by asparagine in IRP2.”
BackgroundInfluentialKrebs, C., Broderick, W. E., Henshaw, T. F., et al. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017562i · Cited by 142 · see citing works
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression
Commichau, F. M., & Stülke, J. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.06071.x · Cited by 140 · see citing works
“Aconitase catalyses the reversible conversion of citrate to isocitrate in the tricarboxylic acid (TCA) cycle and requires an iron-sulphur cluster for activity (Beinert et al., 1996).”
BackgroundChalkley, M. J., Mann, S. I., & DeGrado, W. F. (2021) · Nature Reviews Chemistry · doi:10.1038/s41570-021-00339-5 · Cited by 140 · see citing works
Zhu, Y., Wang, W., Gong, P., Zhao, Y., Pan, Y., Zou, J., Ao, R., Wang, J., Cai, H., Huang, H., et al. (2023) · ACS Nano · doi:10.1021/acsnano.2c11923 · Cited by 136 · see citing works
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Recent Developments in Metal-Catalyzed Additions of Oxygen Nucleophiles to Alkenes and Alkynes
Hintermann, L. (2010) · Topics in organometallic chemistry · doi:10.1007/978-3-642-12073-2_6 · Cited by 133 · see citing works
Bulteau, A., Lundberg, K. C., Ikeda‐Saito, M., Isaya, G., & Szweda, L. I. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501519102 · Cited by 131 · see citing works
Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli
Cunningham, L., Gruer, M. J., & Guest, J. R. (1997) · Microbiology · doi:10.1099/00221287-143-12-3795 · Cited by 128 · see citing works
“It is a monomeric enzyme containing an unstable [4Fe-4S] cluster which is reversibly converted to an inactive [3Fe-4S] form (Beinert et al., 1996).”
BackgroundBrazzolotto, X., Gaillard, J., Pantopoulos, K., Hentze, M. W., & Moulis, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21625 · Cited by 123 · see citing works
The distribution of elements in cells
Williams, R. J., & da Silva, J. J. R. F. (2000) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)00324-6 · Cited by 124 · see citing works
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Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression
Tang, Y., Quail, M. A., Artymiuk, P. J., Guest, J. R., & Green, J. D. (2002) · Microbiology · doi:10.1099/00221287-148-4-1027 · Cited by 115 · see citing works
“…activity (c-Acn) by assembling [4Fe– 4S] clusters under conditions of iron sufficiency, but during iron-starvation and oxidative stress, when the clusters are disassembled, the catalytic activity is lost and the apo-proteins acquire site-specific RNA-binding activity (IRP1) (Beinert et al., 1996).”
BackgroundInfluentialGrove, T. L., Lee, K.-H., Clair, J. S., Krebs, C., & Booker, S. J. (2008) · Biochemistry · doi:10.1021/bi8004297 · Cited by 115 · see citing works
“In this mechanism, one of the remaining two Fe/S clusters is ligated by only three cysteines, providing an open coordination site to which the hydroxyl group of the target seryl residue can bind, which is found in aconitase (65) and proposed in serine dehydratase (66) and other Fe/S cluster-dependent enzymes within th…”
BackgroundWalsby, C. J., Ortillo, D., Yang, J., Nnyepi, M. R., Broderick, W. E., Hoffman, B. M., & Broderick, J. B. (2005) · Inorganic Chemistry · doi:10.1021/ic0484811 · Cited by 114 · see citing works
A Radical Intermediate in Tyrosine Scission to the CO and CN − Ligands of FeFe Hydrogenase
Kuchenreuther, J. M., Myers, W. K., Stich, T. A., George, S. J., NejatyJahromy, Y., Swartz, J. R., & Britt, R. D. (2013) · Science · doi:10.1126/science.1241859 · Cited by 114 · see citing works
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Transcription Factor NsrR from Bacillus subtilis Senses Nitric Oxide with a 4Fe−4S Cluster
Yukl, E. T., Elbaz, M. A., NAKANO, M. M., & Moënne‐Loccoz, P. (2008) · Biochemistry · doi:10.1021/bi801342x · Cited by 110 · see citing works
“by interacting with iron responsive elements (IREs) (18-20).”
Direct Evidence for Metabolon Formation and Substrate Channeling in Recombinant TCA Cycle Enzymes
Bulutoglu, B., Garcia, K. E., Wu, F., Minteer, S. D., & Banta, S. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00523 · Cited by 112 · see citing works
Rethinking the Nitrogenase Mechanism: Activating the Active Site
Buscagan, T. M., & Rees, D. C. (2019) · Joule · doi:10.1016/j.joule.2019.09.004 · 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
Response to the increase of oxidative stress and mutation of mitochondrial DNA in aging
Ma, Y., Wu, S., Lee, W.-Y., Cheng, J.-S., & Wei, Y. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.012 · Cited by 105 · see citing works
Jakimowicz, P., Cheesman, M. R., Bishai, W. R., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412622200 · Cited by 106 · see citing works
Reid, A. N., Pandey, R., Palyada, K., Naikare, H. K., & Stintzi, A. P. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01507-07 · Cited by 105 · see citing works
“coli and Bacillus, aconitases can act as iron and oxidative stress-responsive regulators, binding mRNA and altering transcript stability (1, 13, 52, 96, 98).”
BackgroundNgo, J. K., & Davies, K. J. A. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1404.015 · Cited by 104 · see citing works
Feng, Y., Zhong, N., Rouhier, N., Hase, T., Kusunoki, M., Jacquot, J., Jin, C., & Xia, B. (2006) · Biochemistry · doi:10.1021/bi060444t · Cited by 104 · see citing works
Iron-Dependent RNA-Binding Activity of <i>Mycobacterium tuberculosis</i> Aconitase
Banerjee, S., Nandyala, A. K., Raviprasad, P., Ahmed, N., & Hasnain, S. E. (2007) · Journal of Bacteriology · doi:10.1128/jb.00026-07 · Cited by 98 · see citing works
“The iron-sulfur clusters of these proteins not only participate in electron transport during reversible isomerization of citrate and isocitrate in citric acid cycle (7) but also serve as iron and oxygen sensors of the cell (6, 23).”
BackgroundMiddaugh, J., Hamel, R. D., Jean-Baptiste, G., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411979200 · Cited by 97 · see citing works
Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)
JORDAN, P. A., Tang, Y., Bradbury, A. J., THOMSON, A. J., & Guest, J. R. (1999) · Biochemical Journal · doi:10.1042/bj3440739 · Cited by 97 · see citing works
The selective addition of water to CC bonds; enzymes are the best chemists
Jin, J., & Hanefeld, U. (2011) · Chemical Communications · doi:10.1039/c0cc04153j · Cited by 97 · see citing works
The mechanism of aconitase: 1.8 Å resolution crystal structure of the S642A:citrate complex
Lloyd, S. J., Lauble, H., Prasad, G. S., & Stout, C. D. (1999) · Protein Science · doi:10.1110/ps.8.12.2655 · Cited by 95 · see citing works
“The heart mitochondrial enzyme has been extensively characterized by crystallographic, biochemical, spectroscopic, and kinetic methods~Kennedy & Stout, 1992; Beinert et al., 1996!, providing a model system for understanding the role of @Fe-”
BackgroundMethodSelf-citationDeRose, V. J., Telser, J., Anderson, M. E., et al. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9731480 · Cited by 94 · see citing works
Wecksler, S. R., Stoll, S., Tran, H. T. T., Magnússon, Ó. Þ., Wu, S., King, D., Britt, R. D., & Klinman, J. P. (2009) · Biochemistry · doi:10.1021/bi900918b · Cited by 93 · see citing works
“It is clear from the spectral shape and g values that this species is not a [3Fe-4S] cluster (30), but whether the species is a [4Fe-4S] or [4Fe-4S] cluster is still unknown.”
BackgroundInfluentialCoenzyme A corrects pathological defects in human neurons of PANK2‐associated neurodegeneration
Orellana, D. I., Santambrogio, P., Rubio, A., Yekhlef, L., Cancellieri, C., Dusi, S., Giannelli, S. G., Venco, P., Mazzara, P. G., Cozzi, A., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606391 · Cited by 93 · see citing works
Modeling of the molybdenum center in the nitrogenase FeMo-cofactor
Barrière, F. (2003) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(02)00183-2 · Cited by 93 · see citing works
- Authors
- Beinert, H., Kennedy, M. C., & Stout, C. D.
- Affiliations
- Scripps Research Institute (US)
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 96
- Issue
- 7
- Pages
- 2335-2374
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2089119194
- Cited by
- 606
- References
- 177
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 20 · 2023: 24 · 2022: 22 · 2021: 17 · 2020: 16 · 2019: 24 · 2018: 11 · 2017: 14 · 2016: 28 · 2015: 22 · 2014: 25 · 2013: 19 · 2012: 22
- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- 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
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- aconitase, iron-sulfur clusters, iron-sulfur proteins, iron regulation, iron regulatory proteins, enzyme mechanism, cluster chemistry
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