mossbauer spectroscopy


Summary: A spectroscopic technique which uses the Mossbauer effect (inelastic scattering of gamma radiation resulting from interaction with heavy nuclei) to monitor the small variations in the interaction between an atomic nucleus and its environment. Such variations may be induced by changes in temperature, pressure, chemical state, molecular conformation, molecular interaction, or physical site. It is particularly useful for studies of structure-activity relationship in metalloproteins, mobility of heavy metals, and the state of whole tissue and cell membranes.

Top Publications

  1. Ohki Y, Sunada Y, Honda M, Katada M, Tatsumi K. Synthesis of the P-cluster inorganic core of nitrogenases. J Am Chem Soc. 2003;125:4052-3 pubmed
    ..The structure of the complex isolated therefrom closely resembles that of the reduced form (PN) of the P-clusters, while the 6Fe(II)2Fe(III) oxidation state was manifested by the Mössbauer study. ..
  2. Wu C, Jiang W, Krebs C, Stubbe J. YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase. Biochemistry. 2007;46:11577-88 pubmed
    ..The titrations and kinetic studies provide the first evidence for a protein involved in the maintenance pathway and likely the biosynthetic pathway. ..
  3. Barthelme D, Scheele U, Dinkelaker S, Janoschka A, MacMillan F, Albers S, et al. Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1. J Biol Chem. 2007;282:14598-607 pubmed
    ..Notably, a lethal mutation of the cysteine at position 4 can be rescued by ligand swapping with an adjacent, extra cysteine conserved among all eukaryotes. ..
  4. Abdul Tehrani H, Hudson A, Chang Y, Timms A, Hawkins C, Williams J, et al. Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. J Bacteriol. 1999;181:1415-28 pubmed
    ..In addition to repressing the iron acquisition systems, Fur appears to regulate the demand for iron, probably by controlling the expression of iron-containing proteins. The role of Bfr remains unclear. ..
  5. Tong W, Jameson G, Huynh B, Rouault T. Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster. Proc Natl Acad Sci U S A. 2003;100:9762-7 pubmed
  6. Jameson G, Walters E, Manieri W, Schürmann P, Johnson M, Huynh B. Spectroscopic evidence for site specific chemistry at a unique iron site of the [4Fe-4S] cluster in ferredoxin:thioredoxin reductase. J Am Chem Soc. 2003;125:1146-7 pubmed
  7. Goetz W, Bertelsen P, Binau C, Gunnlaugsson H, Hviid S, Kinch K, et al. Indication of drier periods on Mars from the chemistry and mineralogy of atmospheric dust. Nature. 2005;436:62-5 pubmed
    ..The presence of olivine indicates that liquid water did not play a dominant role in the processes that formed the atmospheric dust. ..
  8. Pierik A, Hagen W, Dunham W, Sands R. Multi-frequency EPR and high-resolution Mössbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Characterization of a supercluster and superspin model protein. Eur J Biochem. 1992;206:705-19 pubmed
    ..8 fractional enrichment in 57Fe, as determined with inductively coupled plasma mass spectrometry.(ABSTRACT TRUNCATED AT 400 WORDS)..
  9. Khan M, Baloch M, Ashfaq M. Spectral analysis and in vitro cytotoxicity profiles of novel organotin(IV) esters of 2-maleimidopropanoic acid. J Enzyme Inhib Med Chem. 2007;22:343-50 pubmed
    ..The title complexes have been screened in vitro for anti-tumour, anti-fungal, anti-leishmanial and urease inhibition activities and displayed promising results. ..

More Information


  1. McSween H, Arvidson R, Bell J, Blaney D, Cabrol N, Christensen P, et al. Basaltic rocks analyzed by the Spirit Rover in Gusev Crater. Science. 2004;305:842-5 pubmed
    ..Mössbauer, Pancam, and Mini-TES spectra confirm the presence of olivine, magnetite, and probably pyroxene. These basalts extend the known range of rock compositions composing the martian crust. ..
  2. Berry J, DeBeer George S, Neese F. Electronic structure and spectroscopy of "superoxidized" iron centers in model systems: theoretical and experimental trends. Phys Chem Chem Phys. 2008;10:4361-74 pubmed publisher
  3. Tse Sum Bui B, Benda R, Schünemann V, Florentin D, Trautwein A, Marquet A. Fate of the (2Fe-2S)(2+) cluster of Escherichia coli biotin synthase during reaction: a Mössbauer characterization. Biochemistry. 2003;42:8791-8 pubmed
    ..This is consistent with the hypothesis that the reduced (4Fe-4S) cluster is involved in mediating the cleavage of AdoMet and that the (2Fe-2S)(2+) is the sulfur source for biotin. ..
  4. Miao R, Martinho M, Morales J, Kim H, Ellis E, Lill R, et al. EPR and Mössbauer spectroscopy of intact mitochondria isolated from Yah1p-depleted Saccharomyces cerevisiae. Biochemistry. 2008;47:9888-99 pubmed publisher
    ..EPR, Mossbauer spectroscopy, and electron microscopy were used to characterize the Fe that accumulates in Yah1p-depleted isolated ..
  5. Ling Y, Zhang Y. Mössbauer, NMR, geometric, and electronic properties in S = 3/2 iron porphyrins. J Am Chem Soc. 2009;131:6386-8 pubmed publisher
    ..These results should facilitate future investigations of related heme proteins and model systems. ..
  6. Kopriva S, Büchert T, Fritz G, Suter M, Benda R, Schünemann V, et al. The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation. J Biol Chem. 2002;277:21786-91 pubmed
    ..We conclude, therefore, that the presence of an iron-sulfur cluster determines the APS specificity of the sulfate-reducing enzymes and thus separates the APS- and PAPS-dependent assimilatory sulfate reduction pathways. ..
  7. Huggins F, Bali S, Huffman G, Eyring E. Iron-oxide aerogel and xerogel catalyst formulations: characterization by 57Fe Mössbauer and XAFS spectroscopies. Spectrochim Acta A Mol Biomol Spectrosc. 2010;76:74-83 pubmed publisher
  8. Popescu V, Munck E, Fox B, Sanakis Y, Cummings J, Turner I, et al. Mössbauer and EPR studies of the photoactivation of nitrile hydratase. Biochemistry. 2001;40:7984-91 pubmed
    ..We also describe preliminary EPR photolysis studies that have yielded new intermediates. ..
  9. Kröckel M, Trautwein A, Arendsen A, Hagen W. The prismane protein resolved--Mössbauer investigation of a 4Fe cluster with an unusual mixture of bridging ligands and metal coordinations. Eur J Biochem. 1998;251:454-61 pubmed
    ..H., Liu, M.-Y. & LeGall, J. (1992) J. Biol. Chem. 287, 4487-4496]. However, they are in full agreement with the crystal structure of the isolated protein, which, concurrent with our Mössbauer investigation, has been solved. ..
  10. Muller K, Matzanke B, Schunemann V, Trautwein A, Hantke K. FhuF, an iron-regulated protein of Escherichia coli with a new type of [2Fe-2S] center. Eur J Biochem. 1998;258:1001-8 pubmed
    ..The phenotype of fhuF mutants and the structural features of the FhuF protein suggest that FhuF is involved in the reduction of ferric iron in cytoplasmic ferrioxamine B. ..
  11. Foster M, Bian S, Surerus K, Cowan J. Elucidation of a [4Fe-4S] cluster degradation pathway: rapid kinetic studies of the degradation of Chromatium vinosum HiPIP. J Biol Inorg Chem. 2001;6:266-74 pubmed
    ..Consistent results are obtained from absorption, fluorescence, Mössbauer and EPR measurements...
  12. Eser B, Barr E, Frantom P, Saleh L, Bollinger J, Krebs C, et al. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. J Am Chem Soc. 2007;129:11334-5 pubmed
  13. Walker F, Licoccia S, Paolesse R. Iron corrolates: unambiguous chloroiron(III) (corrolate)(2-.) pi-cation radicals. J Inorg Biochem. 2006;100:810-37 pubmed not relevant to the high-valent reactivity of the complex. ..
  14. Upadhyay A, Hooper A, Hendrich M. NO reductase activity of the tetraheme cytochrome C554 of Nitrosomonas europaea. J Am Chem Soc. 2006;128:4330-7 pubmed
    ..The NO reductase activity of cyt c(554) may be important during ammonia oxidation in N. europaea at low oxygen concentrations to detoxify NO produced by reduction of nitrite or incomplete oxidation of hydroxylamine...
  15. Reger D, Gardinier J, Elgin J, Smith M, Hautot D, Long G, et al. Structure-function correlations in Iron(II) tris(pyrazolyl)borate spin-state crossover complexes. Inorg Chem. 2006;45:8862-75 pubmed
  16. B nisch H, Schmidt C, Bianco P, Ladenstein R. Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S. Acta Crystallogr D Biol Crystallogr. 2005;61:990-1004 pubmed publisher
  17. Layer G, Grage K, Teschner T, Schünemann V, Breckau D, Masoumi A, et al. Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines. J Biol Chem. 2005;280:29038-46 pubmed
    ..The reported significant correlation of structural and functional biophysical and biochemical data identifies HemN as a useful model system for the elucidation of general AdoMet radical enzyme features. ..
  18. Oshtrakh M. Mössbauer spectroscopy in biomedical research. Faraday Discuss. 2004;126:119-40; discussion 169-83 pubmed
    ..The results obtained may be useful for further understanding of the molecular nature of diseases and pathological processes. ..
  19. Seguin A, Sutak R, Bulteau A, Garcia Serres R, Oddou J, Lefevre S, et al. Evidence that yeast frataxin is not an iron storage protein in vivo. Biochim Biophys Acta. 2010;1802:531-8 pubmed publisher
    ..Our results do not privilege the hypothesis of Yfh1p being an iron storage protein in vivo. ..
  20. Miao R, Kim H, Koppolu U, Ellis E, Scott R, Lindahl P. Biophysical characterization of the iron in mitochondria from Atm1p-depleted Saccharomyces cerevisiae. Biochemistry. 2009;48:9556-68 pubmed publisher
    ..In this study the nature of the accumulated Fe was examined using Mossbauer spectroscopy, EPR, electronic absorption spectroscopy, X-ray absorption spectroscopy, and electron microscopy...
  21. Vrajmasu V, Bominaar E, Meyer J, Munck E. Mössbauer study of reduced rubredoxin as purified and in whole cells. Structural correlation analysis of spin Hamiltonian parameters. Inorg Chem. 2002;41:6358-71 pubmed
    ..These findings establish Mössbauer spectroscopy as a structural tool for investigating iron sites in whole cells. ..
  22. Silvestri A, Ruisi G, Girasolo M. The dynamics of 57Fe nuclei in Fe(II)-DNA and [Fe(II)(1-methyl-2-mercaptoimidazole)2]-DNA condensates. J Inorg Biochem. 2002;92:171-6 pubmed
  23. Wile B, Trovitch R, Bart S, Tondreau A, Lobkovsky E, Milsmann C, et al. Reduction chemistry of aryl- and alkyl-substituted bis(imino)pyridine iron dihalide compounds: molecular and electronic structures of [(PDI)2Fe] derivatives. Inorg Chem. 2009;48:4190-200 pubmed publisher
    ..Thus, the two-electron reduction of the diamagnetic, low-spin complex [(PDI)2Fe]2+ to [(PDI)2Fe] is ligand-based with a concomitant spin change at iron. ..
  24. Yun D, Garcia Serres R, Chicalese B, An Y, Huynh B, Bollinger J. (Mu-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry. 2007;46:1925-32 pubmed
  25. Mbughuni M, Chakrabarti M, Hayden J, Bominaar E, Hendrich M, Munck E, et al. Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proc Natl Acad Sci U S A. 2010;107:16788-93 pubmed publisher
    ..Our results demonstrate facile electron transfer between Fe(II), O(2), and the organic ligand, thereby supporting the proposed wild-type enzyme mechanism. ..
  26. Wiatrowski H, Das S, Kukkadapu R, Ilton E, Barkay T, Yee N. Reduction of Hg(II) to Hg(0) by magnetite. Environ Sci Technol. 2009;43:5307-13 pubmed
    ..These results suggest that Hg(II) reaction with solid-phase Fe(II) is a kinetically favorable pathway for Hg(II) reduction in magnetite-hearing environmental systems. ..
  27. Hoffart L, Barr E, Guyer R, Bollinger J, Krebs C. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. Proc Natl Acad Sci U S A. 2006;103:14738-43 pubmed
    ..The close correspondence of the accumulating states in the P4H and TauD reactions supports the hypothesis of a conserved mechanism for substrate hydroxylation by enzymes in this family. ..
  28. Baldwin J, Voegtli W, Khidekel N, Moenne Loccoz P, Krebs C, Pereira A, et al. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. J Am Chem Soc. 2001;123:7017-30 pubmed
    ..The reprogramming to F208 monooxygenase requires both amino acid substitutions, as very little epsilon-hydroxyphenylalanine is formed and pathways leading to Y122* formation predominate in both R2-D84E and R2-W48F. ..
  29. Armelao L, Schiavon G, Seraglia R, Tondello E, Russo U, Traldi P. Electrospray ionization mass spectrometric study of the hydrolysis-polycondensation process of Sn(OBu(t))(4). Rapid Commun Mass Spectrom. 2001;15:1855-61 pubmed
    ..Mössbauer spectroscopy has elucidated the fast behavior of the hydrolytic oligomerization process, while calorimetric data have demonstrated the high enthalpy of the reaction in the presence of different solvents. ..
  30. Price J, Barr E, Hoffart L, Krebs C, Bollinger J. Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry. 2005;44:8138-47 pubmed
    ..g., temperature), protein mutagenesis, the use of substrate analogues, or some combination of these. ..
  31. Hänzelmann P, Hernandez H, Menzel C, Garcia Serres R, Huynh B, Johnson M, et al. Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. J Biol Chem. 2004;279:34721-32 pubmed
  32. Cosper M, Jameson G, Hernandez H, Krebs C, Huynh B, Johnson M. Characterization of the cofactor composition of Escherichia coli biotin synthase. Biochemistry. 2004;43:2007-21 pubmed
    ..In addition, they provide a firm foundation for assessing cluster transformations that occur during turnover and the catalytic competence of the [2Fe-2S](2+) cluster as the immediate S-donor for biotin biosynthesis. ..
  33. Fredrickson J, Kota S, Kukkadapu R, Liu C, Zachara J. Influence of electron donor/acceptor concentrations on hydrous ferric oxide (HFO) bioreduction. Biodegradation. 2003;14:91-103 pubmed
    ..The respiration driven rate of Fe(II) formation from HFO is believed to be a primary factor governing the array of ferrous and ferric iron phases formed during reduction. ..
  34. Elgren T, Lynch J, Juarez Garcia C, Munck E, Sjoberg B, Que L. Electron transfer associated with oxygen activation in the B2 protein of ribonucleotide reductase from Escherichia coli. J Biol Chem. 1991;266:19265-8 pubmed
    ..9 mol-equivalents of Fe(II) are oxidized per mol of O2 consumed. Our stoichiometry data has led us to propose a model for dioxygen activation catalyzed by RRB2 which invokes electron transfer between iron clusters. ..
  35. Makris T, Chakrabarti M, Munck E, Lipscomb J. A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis. Proc Natl Acad Sci U S A. 2010;107:15391-6 pubmed publisher
    ..Notably, CmlA homologs are widely distributed in natural product biosynthetic pathways, including a variety of pharmaceutically important beta-hydroxylated antibiotics and cytostatics. ..
  36. Park C, Walker J, Tannenbaum R, Stiegman A, Frydrych J, Machala L. Sol-gel-derived iron oxide thin films on silicon: surface properties and interfacial chemistry. ACS Appl Mater Interfaces. 2009;1:1843-6 pubmed publisher
    ..of films into a ternary layered structure with iron oxide, Fe(2)O(3), at the surface, characterized by Mossbauer spectroscopy, and reduced, metallic iron characterized by depth profiling of the surface by X-ray photoelectron ..
  37. Jang J, Brantley S. Investigation of Wüstite (FeO) dissolution: implications for reductive dissolution of ferric oxides. Environ Sci Technol. 2009;43:1086-90 pubmed
  38. Chen H, Ikeda Saito M, Shaik S. Nature of the Fe-O2 bonding in oxy-myoglobin: effect of the protein. J Am Chem Soc. 2008;130:14778-90 pubmed publisher
    ..The VB model is generalized, showing how the protein or the axial ligand of the oxyheme complex can determine the nature of its bonding in terms of the blend of the three bonding models: Weiss, Pauling, and McClure-Goddard. ..
  39. Neese F. Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mössbauer properties. Curr Opin Chem Biol. 2003;7:125-35 pubmed
  40. Doster W. The dynamical transition of proteins, concepts and misconceptions. Eur Biophys J. 2008;37:591-602 pubmed publisher
    ..Finally, the role of fast hydrogen bond fluctuations contributing to the amplitude enhancement is discussed. ..
  41. Yoon S, Lippard S. Water affects the stereochemistry and dioxygen reactivity of carboxylate-rich diiron(II) models for the diiron centers in dioxygen-dependent non-heme enzymes. J Am Chem Soc. 2005;127:8386-97 pubmed
    ..2(HO(2)CAr(Tol)) (6) and [Fe(6)(mu-O)(2)(mu-OH)(4)(mu-O(2)CAr(Tol))(6)(4-NCC(5)H(4)N)(4)Cl(2)] (7). ..
  42. Bomatí Miguel O, Tartaj P, Morales M, Bonville P, Golla Schindler U, Zhao X, et al. Core-shell iron-iron oxide nanoparticles synthesized by laser-induced pyrolysis. Small. 2006;2:1476-83 pubmed
  43. Jensen M, Costas M, Ho R, Kaizer J, Mairata i Payeras A, Munck E, et al. High-valent nonheme iron. Two distinct iron(IV) species derived from a common iron(II) precursor. J Am Chem Soc. 2005;127:10512-25 pubmed
    ..The reactivity of 1 with tBuOOH in the two solvents reveals an unexpectedly rich iron(IV) chemistry that can be supported by the BPMCN ligand. ..
  44. Xing G, Hoffart L, Diao Y, Prabhu K, Arner R, Reddy C, et al. A coupled dinuclear iron cluster that is perturbed by substrate binding in myo-inositol oxygenase. Biochemistry. 2006;45:5393-401 pubmed
  45. Kim H, Zatsman A, Upadhyay A, Whittaker M, Bergmann D, Hendrich M, et al. Membrane tetraheme cytochrome c(m552) of the ammonia-oxidizing nitrosomonas europaea: a ubiquinone reductase. Biochemistry. 2008;47:6539-51 pubmed publisher
    ..b>Mossbauer spectroscopy of the reduced (57)Fe-enriched protein revealed the presence of high-spin and low-spin hemes in a 1:3 ..
  46. Zhang X, Furutachi H, Fujinami S, Nagatomo S, Maeda Y, Watanabe Y, et al. Structural and spectroscopic characterization of (mu-hydroxo or mu-oxo)(mu-peroxo)diiron(III) complexes: models for peroxo intermediates of non-heme diiron proteins. J Am Chem Soc. 2005;127:826-7 pubmed
  47. Benetoli L, de Souza C, da Silva K, de Souza I, de Santana H, Paesano A, et al. Amino acid interaction with and adsorption on clays: FT-IR and Mössbauer spectroscopy and X-ray diffractometry investigations. Orig Life Evol Biosph. 2007;37:479-93 pubmed
    ..This means that Cys was able to partially reduce iron present in bentonite. This result is similar to that which occurs with aconitase where the ferric ions are reduced to Fe 2.5. ..
  48. Jankovics H, Nagy L, Buzás N, Pellerito L, Barbieri R. Coordination properties of adenosine-5'-monophosphate and related ligands towards Me2Sn(IV)2+ in aqueous solution. J Inorg Biochem. 2002;92:55-64 pubmed
    ..With increasing pH, the phosphate groups were replaced by the deprotonated alcoholic [O] atoms of the sugar moiety. The solid complex proved to be tbp structure with bidentate phosphate coordination. ..
  49. Wu S, Wu G, Surerus K, Cowan J. Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate. Biochemistry. 2002;41:8876-85 pubmed
    ..Fully oxidized cluster appears to be the natural state for transfer to target proteins. Reduced Fd does not readily reduce ISU-bound [2Fe-2S](2+) and does not promote cluster transfer to an apo Fd target. ..
  50. Egan T, Combrinck J, Egan J, Hearne G, Marques H, Ntenteni S, et al. Fate of haem iron in the malaria parasite Plasmodium falciparum. Biochem J. 2002;365:343-7 pubmed
    ..Of this, 88+/-9% is in the form of haemozoin. (57)Fe-Mössbauer spectroscopy shows that haemozoin is the only detectable iron species in trophozoites. Electron spectroscopic imaging confirms this conclusion. ..
  51. Horner O, Oddou J, Mouesca J, Jouve H. Mössbauer identification of a protonated ferryl species in catalase from Proteus mirabilis: density functional calculations on related models. J Inorg Biochem. 2006;100:477-9 pubmed
    ..Rovira, I. Fita, J. Phys. Chem. B 107 (2003) 5300-5305]. Therefore, we attribute the LpH II compound to a protonated ferryl Fe(IV)-OH complex, whereas the HpH II compound corresponds to the classical ferryl Fe(IV)O complex. ..
  52. Pereira A, Tavares P, Moura I, Moura J, Huynh B. Mössbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase. J Am Chem Soc. 2001;123:2771-82 pubmed
    ..The results also reveal that binding of exogenous CO to the H cluster affects significantly the exchange coupling between the [4Fe-4S](H) and the [2Fe](H) subclusters. Implication of such a CO binding effect is discussed. ..
  53. Saalfrank R, Prakash R, Maid H, Hampel F, Heinemann F, Trautwein A, et al. Synthesis and characterization of metal-centered, six-membered, mixed-valent, heterometallic wheels of iron, manganese, and indium. Chemistry. 2006;12:2428-33 pubmed
    ..In 2, three Mn(II) ions alternate with three In(III) ions, whereas in 3, four In(III) ions are arranged in pairs and alternate with one Mn(II) ion each. In 2 and 3 an Mn(II) ion is encapsulated in the center...