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Chemical Compound Review

IRON     iron

Synonyms: Feronate, Ferretts, Hemocyte, Yieronia, Feratab, ...
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Disease relevance of iron

  • This approach to the use of an insoluble electron acceptor may explain why Geobacter species predominate over other Fe(III) oxide-reducing microorganisms in a wide variety of sedimentary environments [1].
  • Fe(III)-reducing microorganisms in the genus Shewanella have resolved this problem by releasing soluble quinones that can carry electrons from the cell surface to Fe(III) oxide that is at a distance from the cell [1].
  • Surprisingly, even Thermotoga maritima, previously considered to have only a fermentative metabolism, could grow as a respiratory organism when Fe(III) was provided as an electron acceptor [2].
  • Therefore, we studied the effects of experimental iron overload on hepatocyte lysosomal structure, physicochemical properties, and function in rats fed carbonyl iron [3].
  • One of the two nonidentical subunits of Escherichia coli ribonucleotide reductase, protein B2, contains in its active form two antiferromagnetically coupled Fe(III) ions and an organic free radical that arises by the one-electron oxidation of tyrosine-122 of the polypeptide chain [4].

Psychiatry related information on iron

  • Abeta binds Zn(2+), Cu(2+), and Fe(3+) in vitro, and these metals are markedly elevated in the neocortex and especially enriched in amyloid plaque deposits of individuals with Alzheimer's disease (AD) [5].
  • It subsequently decays within 10 s to form a mu-oxodiFe(III)-protein complex (species D), which partially vacates the ferroxidase sites of the protein to generate Fe(III) clusters (species C) at a reaction time of 10 min [6].

High impact information on iron

  • Importantly, binding to AHSP facilitates the conversion of oxy-alphaHb to a deoxygenated, oxidized [Fe(III)], nonreactive form in which all six coordinate positions are occupied [7].
  • Geobacter metallireducens accesses insoluble Fe(III) oxide by chemotaxis [1].
  • Our results suggest that increasing the bioavailability of Fe(III) by adding suitable ligands provides a potential alternative to oxygen addition for the bioremediation of petroleum-contaminated aquifers [8].
  • Plasma transferrins are monomeric glycoproteins with a molecular weight of approximately 80,000 (ref. 2); they have two similar and very strong binding sites for Fe(III), together with two associated anion binding sites [9].
  • Because imidazole compounds such as histamine can interact with Fe(III) heme proteins, we investigated whether such substances could interact with Rhodnius nitrophorins [10].

Chemical compound and disease context of iron


Biological context of iron

  • Here we report that adding organic ligands that bind to Fe(III) dramatically increases its bioavailability, and that in the presence of these ligands, rates of degradation of aromatic hydrocarbons in anoxic aquifer sediments are comparable to those in oxic sediments [8].
  • We investigated whether lipid peroxidation occurred in rats fed a diet containing 3% carbonyl iron for 5-13 wk, and if this resulted in the formation of MDA- and 4-HNE- protein adducts [16].
  • ADCC activity was found primarily in the plastic nonadherent cell population and was greatly enriched following removal of phagocytic cells by carbonyl iron [17].
  • Carbonyl iron had no effect on blood alcohol concentration, hepatic biochemical measurements, or liver histology in control animals [18].
  • Iron (Fe) is critical for cell-cycle progression and DNA synthesis and potentially represents a novel molecular target for the design of new anticancer agents [19].

Anatomical context of iron

  • Removal of macrophages from adherent splenocytes by either carbonyl-iron incubation or passage through Sephadex G-10 columns did not affect their synergistic function [20].
  • Pretreatment of spleen cells with carbonyl iron and a magnet did not abrogate the suppressor cell function [21].
  • Two new techniques were developed that separate monocytes into M1 + M2 and M3 fractions; one used preferential incorporation of carbonyl iron particles by M3 cells and the other used the selective aggregation of M3 cells by thrombin in the presence of platelets [22].
  • These studies have examined the role of iron in intact hepatocytes using cells from rats fed an iron-deficient diet, a control diet or a diet containing 3% carbonyl iron [23].
  • The isolated membranes contributed to the reduction of anthracycline-bound Fe(III) and probably represented the main determinant of lipid peroxidation by iron-Dnr [24].

Associations of iron with other chemical compounds

  • Superoxide dismutase activity, glutathione peroxidase activity, and reduced glutathione concentrations, together with malondialdehyde production, were measured in the livers of rats chronically iron-overloaded by (a) parenteral iron (primarily Kupffer cell iron deposition) and (b) dietary carbonyl iron (mainly parenchymal iron deposition) [25].
  • First, MAC1 is involved in basal level transcription of FRE1, encoding a plasma membrane component associated with both Cu(II) and Fe(III) reduction [26].
  • The rationalization of this fact, and the possible explanation of a great accumulation of spectroscopic data, is that cytochrome a3 may be a two-electron redox center, with stable Fe(IV), Fe(III), and Fe(II) states during its redox cycle [27].
  • An independent hypothesis holds that in Cryptococcus neoformans, an important function of the melanizing enzyme (apart from melanization) is the oxidation of Fe(II) to Fe(III), thereby forestalling generation of the harmful hydroxyl radical from H(2)O(2) [28].
  • A model for the structure of this inhibitor-enzyme complex is proposed in which the 5-androstene ring system of the steroid occupies the substrate binding site, and the amine group of the side chain occupies an axial coordination position of the Fe(III) center [29].

Gene context of iron


Analytical, diagnostic and therapeutic context of iron

  • Internal electron transfer from the [(NH3)5RuII-] centre to the Fe(III) haem centre occurs with a rate constant k congruent to 53 s-1 (25 degrees C) (delta H = 3.5 kcal mol-1, delta S = -39 EU), as measured by pulse radiolysis [35].
  • The nature of bonding interactions between Fe(III) and NO in the ferric nitrosyl complexes of myoglobin (Mb), hemoglobin A (HbA), and horseradish peroxidase (HRP) is investigated by Soret-excited resonance Raman spectroscopy [36].
  • Gel electrophoretic mobility-shift assays show that Fe(2+) and not Fe(3+) activates DtxR for DNA binding [37].
  • Treatment of lymphocyte preparations with carbonyl iron and magnetic separation to remove phagocytic cells or treatment with complement-coated red cells followed by repeated gradient centrifugation to remove complement receptor-bearing lymphocytes did not reduce the granulocytotoxicity [38].
  • In contrast, the active Fe(II) + CO forms of both wild-type and M124R CooA are six-coordinate and low-spin with a protein ligand other than Cys(75), so that WT and Fe(III) M124R CooA are apparently achieving an active conformation despite two different heme coordination and ligation states [39].


  1. Geobacter metallireducens accesses insoluble Fe(III) oxide by chemotaxis. Childers, S.E., Ciufo, S., Lovley, D.R. Nature (2002) [Pubmed]
  2. Microbiological evidence for Fe(III) reduction on early Earth. Vargas, M., Kashefi, K., Blunt-Harris, E.L., Lovley, D.R. Nature (1998) [Pubmed]
  3. Alterations in the structure, physicochemical properties, and pH of hepatocyte lysosomes in experimental iron overload. Myers, B.M., Prendergast, F.G., Holman, R., Kuntz, S.M., LaRusso, N.F. J. Clin. Invest. (1991) [Pubmed]
  4. Superoxide dismutase participates in the enzymatic formation of the tyrosine radical of ribonucleotide reductase from Escherichia coli. Eliasson, R., Jörnvall, H., Reichard, P. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  5. Evidence that the beta-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of abeta by zinc. Cuajungco, M.P., Goldstein, L.E., Nunomura, A., Smith, M.A., Lim, J.T., Atwood, C.S., Huang, X., Farrag, Y.W., Perry, G., Bush, A.I. J. Biol. Chem. (2000) [Pubmed]
  6. mu-1,2-Peroxobridged di-iron(III) dimer formation in human H-chain ferritin. Bou-Abdallah, F., Papaefthymiou, G.C., Scheswohl, D.M., Stanga, S.D., Arosio, P., Chasteen, N.D. Biochem. J. (2002) [Pubmed]
  7. Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin. Feng, L., Gell, D.A., Zhou, S., Gu, L., Kong, Y., Li, J., Hu, M., Yan, N., Lee, C., Rich, A.M., Armstrong, R.S., Lay, P.A., Gow, A.J., Weiss, M.J., Mackay, J.P., Shi, Y. Cell (2004) [Pubmed]
  8. Stimulated anoxic biodegradation of aromatic hydrocarbons using Fe(III) ligands. Lovley, D.R., Woodward, J.C., Chapelle, F.H. Nature (1994) [Pubmed]
  9. Evidence for the bilobal nature of diferric rabbit plasma transferrin. Gorinsky, B., Horsburgh, C., Lindley, P.F., Moss, D.S., Parkar, M., Watson, J.L. Nature (1979) [Pubmed]
  10. High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus. Ribeiro, J.M., Walker, F.A. J. Exp. Med. (1994) [Pubmed]
  11. Hepatic lipid peroxidation in vivo in rats with chronic iron overload. Bacon, B.R., Tavill, A.S., Brittenham, G.M., Park, C.H., Recknagel, R.O. J. Clin. Invest. (1983) [Pubmed]
  12. Carbonyl iron therapy for iron deficiency anemia. Gordeuk, V.R., Brittenham, G.M., McLaren, C.E., Hughes, M.A., Keating, L.J. Blood (1986) [Pubmed]
  13. Hepatic mitochondrial oxidative metabolism and lipid peroxidation in experimental hexachlorobenzene-induced porphyria with dietary carbonyl iron overload. Feldman, E.S., Bacon, B.R. Hepatology (1989) [Pubmed]
  14. Peroxidase activity of cyclooxygenase-2 (COX-2) cross-links beta-amyloid (Abeta) and generates Abeta-COX-2 hetero-oligomers that are increased in Alzheimer's disease. Nagano, S., Huang, X., Moir, R.D., Payton, S.M., Tanzi, R.E., Bush, A.I. J. Biol. Chem. (2004) [Pubmed]
  15. Fe(III).ATP complexes. Models for ferritin and other polynuclear iron complexes with phosphate. Mansour, A.N., Thompson, C., Theil, E.C., Chasteen, N.D., Sayers, D.E. J. Biol. Chem. (1985) [Pubmed]
  16. Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload. Houglum, K., Filip, M., Witztum, J.L., Chojkier, M. J. Clin. Invest. (1990) [Pubmed]
  17. Immunologic control of a retrovirus-associated murine adenocarcinoma. VIII. Corynebacterium parvum-activated natural killer cells as potent antibody-dependent cell-mediated cytotoxicity effectors. Weinhold, K.J., Bolognesi, D.P., Matthews, T.J. J. Natl. Cancer Inst. (1985) [Pubmed]
  18. Experimental liver cirrhosis induced by alcohol and iron. Tsukamoto, H., Horne, W., Kamimura, S., Niemelä, O., Parkkila, S., Ylä-Herttuala, S., Brittenham, G.M. J. Clin. Invest. (1995) [Pubmed]
  19. A class of iron chelators with a wide spectrum of potent antitumor activity that overcomes resistance to chemotherapeutics. Whitnall, M., Howard, J., Ponka, P., Richardson, D.R. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  20. The in vitro effects of Bordetella pertussis lymphocytosis-promoting factor on murine lymphocytes. III. B-cell dependence for T-cell proliferation. Ho, M.K., Kong, A.S., Morse, S.I. J. Exp. Med. (1979) [Pubmed]
  21. Mechanisms of genetic resistance to Friend virus leukemia. III. Susceptibility of mitogen-responsive lymphocytes mediated by T cells. Kumar, V., Caruso, T., Bennett, M. J. Exp. Med. (1976) [Pubmed]
  22. Volumetric and functional heterogeneity of human monocytes. Arenson, E.B., Epstein, M.B., Seeger, R.C. J. Clin. Invest. (1980) [Pubmed]
  23. Iron mediates production of a neutrophil chemoattractant by rat hepatocytes metabolizing ethanol. Hultcrantz, R., Bissell, D.M., Roll, F.J. J. Clin. Invest. (1991) [Pubmed]
  24. Role of daunosamine and hydroxyacetyl side chain in reaction with iron and lipid peroxidation by anthracyclines. Gianni, L., Viganò, L., Lanzi, C., Niggeler, M., Malatesta, V. J. Natl. Cancer Inst. (1988) [Pubmed]
  25. Effects of iron loading on free radical scavenging enzymes and lipid peroxidation in rat liver. Fletcher, L.M., Roberts, F.D., Irving, M.G., Powell, L.W., Halliday, J.W. Gastroenterology (1989) [Pubmed]
  26. MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. Jungmann, J., Reins, H.A., Lee, J., Romeo, A., Hassett, R., Kosman, D., Jentsch, S. EMBO J. (1993) [Pubmed]
  27. Cytochrome oxidase: an alternative model. Seiter, C.H., Angelos, S.G. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  28. Pathogenic roles for fungal melanins. Jacobson, E.S. Clin. Microbiol. Rev. (2000) [Pubmed]
  29. Proximity of the substrate binding site and the heme-iron catalytic site in cytochrome P-450scc. Sheets, J.J., Vickery, L.E. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  30. Regulation of high affinity iron uptake in the yeast Saccharomyces cerevisiae. Role of dioxygen and Fe. Hassett, R.F., Romeo, A.M., Kosman, D.J. J. Biol. Chem. (1998) [Pubmed]
  31. Expression of the yeast FRE genes in transgenic tobacco. Samuelsen, A.I., Martin, R.C., Mok, D.W., Mok, M.C. Plant Physiol. (1998) [Pubmed]
  32. Synergistic toxicity of iron and arachidonic acid in HepG2 cells overexpressing CYP2E1. Caro, A.A., Cederbaum, A.I. Mol. Pharmacol. (2001) [Pubmed]
  33. Asbestos inhalation induces tyrosine nitration associated with extracellular signal-regulated kinase 1/2 activation in the rat lung. Iwagaki, A., Choe, N., Li, Y., Hemenway, D.R., Kagan, E. Am. J. Respir. Cell Mol. Biol. (2003) [Pubmed]
  34. Inactivation of enzymes and an enzyme inhibitor by oxidative modification with chlorinated amines and metal-catalyzed oxidation systems. Maier, K., Hinze, H., Holzer, H. Biochim. Biophys. Acta (1991) [Pubmed]
  35. Directional electron transfer in ruthenium-modified horse heart cytochrome c. Bechtold, R., Kuehn, C., Lepre, C., Isied, S.S. Nature (1986) [Pubmed]
  36. Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: detection of Fe(III)--NO stretching, Fe(III)--N--O bending, and Fe(II)--N--O bending vibrations. Benko, B., Yu, N.T. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  37. Metal stoichiometry and functional studies of the diphtheria toxin repressor. Spiering, M.M., Ringe, D., Murphy, J.R., Marletta, M.A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  38. Antibody-dependent lymphocyte-mediated granulocyte cytotoxicity in man. Logue, G.L., Kurlander, R., Pepe, P., Davis, W., Silberman, H. Blood (1978) [Pubmed]
  39. Redox-mediated transcriptional activation in a CooA variant. Thorsteinsson, M.V., Kerby, R.L., Youn, H., Conrad, M., Serate, J., Staples, C.R., Roberts, G.P. J. Biol. Chem. (2001) [Pubmed]
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