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MeSH Review

Spectroscopy, Mossbauer

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Disease relevance of Spectroscopy, Mossbauer


High impact information on Spectroscopy, Mossbauer

  • Mossbauer spectroscopy revealed the presence of a four cysteine-coordinated nonoxidizable [2Fe-2S]2+ cluster that bridges two Grx2 molecules via two structural Cys residues to form dimeric holo Grx2 [4].
  • High-pressure Mössbauer spectroscopy on several compositions across the (Mg,Fe)O magnesiowüstite solid solution confirms that ferrous iron (Fe(2+)) undergoes a high-spin to low-spin transition at pressures and for compositions relevant to the bulk of the Earth's mantle [5].
  • Using 57Fe or 56Fe for activation we have studied with Mössbauer spectroscopy the beef heart enzyme in the presence of citrate [6].
  • Mössbauer spectroscopy of anaerobically purified HemN has identified a predominantly [4Fe-4S](2+) cluster in which only three iron atoms were coordinated by cysteine residues (isomer shift of delta = 0.43 (1) mm/s) [7].
  • Mössbauer spectroscopy of whole cells at various states of (57)Fe-labeled chrysobactin uptake showed that this enzyme is not required for iron removal from chrysobactin in vivo [8].

Chemical compound and disease context of Spectroscopy, Mossbauer


Biological context of Spectroscopy, Mossbauer


Anatomical context of Spectroscopy, Mossbauer


Associations of Spectroscopy, Mossbauer with chemical compounds


Gene context of Spectroscopy, Mossbauer


Analytical, diagnostic and therapeutic context of Spectroscopy, Mossbauer

  • The valence of iron doped in the TiO(2), phase formation, defect structures, band gaps, and magnetic properties of the resultant nanopowders were systematically investigated using Mössbauer spectroscopy, XRD, Raman spectroscopy, TEM/HRTEM, UV-vis spectroscopy, and measurements of magnetic properties [23].
  • An unusual discontinuity in the pressure derivatives of C11 and C12 at 4.7+/-0.2 GPa corresponds to the pressure at which the onset of a magnetic ordering transition is observed by high-pressure Mössbauer spectroscopy and neutron powder diffraction [24].
  • Iron mobilization by deferoxamine from iron-loaded rat heart cells in culture was studied by electron microscopy and Mössbauer spectroscopy to identify the chelatable iron pool [25].


  1. Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli. Popescu, C.V., Bates, D.M., Beinert, H., Münck, E., Kiley, P.J. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 2. Mössbauer spectroscopy. Lipscomb, J.D., Andersson, K.K., Münck, E., Kent, T.A., Hooper, A.B. Biochemistry (1982) [Pubmed]
  3. A dimer of the FeS cluster biosynthesis protein IscA from cyanobacteria binds a [2Fe2S] cluster between two protomers and transfers it to [2Fe2S] and [4Fe4S] apo proteins. Wollenberg, M., Berndt, C., Bill, E., Schwenn, J.D., Seidler, A. Eur. J. Biochem. (2003) [Pubmed]
  4. Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor. Lillig, C.H., Berndt, C., Vergnolle, O., Lönn, M.E., Hudemann, C., Bill, E., Holmgren, A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. Iron spin transition in Earth's mantle. Speziale, S., Milner, A., Lee, V.E., Clark, S.M., Pasternak, M.P., Jeanloz, R. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Mössbauer and EPR studies of activated aconitase: development of a localized valence state at a subsite of the [4Fe-4S] cluster on binding of citrate. Emptage, M.H., Kent, T.A., Kennedy, M.C., Beinert, H., Münck, E. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  7. Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines. Layer, G., Grage, K., Teschner, T., Schünemann, V., Breckau, D., Masoumi, A., Jahn, M., Heathcote, P., Trautwein, A.X., Jahn, D. J. Biol. Chem. (2005) [Pubmed]
  8. Chrysobactin-dependent iron acquisition in Erwinia chrysanthemi. Functional study of a homolog of the Escherichia coli ferric enterobactin esterase. Rauscher, L., Expert, D., Matzanke, B.F., Trautwein, A.X. J. Biol. Chem. (2002) [Pubmed]
  9. Escherichia coli iron enterobactin uptake monitored by Mössbauer spectroscopy. Matzanke, B.F., Ecker, D.J., Yang, T.S., Huynh, B.H., Müller, G., Raymond, K.N. J. Bacteriol. (1986) [Pubmed]
  10. Zero-field Mössbauer studies of diferric human transferrin. Kilár, F., Seidel, A.G., Häggström, L. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  11. Mössbauer studies of the non-heme iron and cytochrome b559 in a Chlamydomonas reinhardtii PSI- mutant and their interactions with alpha-tocopherol quinone. Burda, K., Kruk, J., Borgstädt, R., Stanek, J., Strzałka, K., Schmid, G.H., Kruse, O. FEBS Lett. (2003) [Pubmed]
  12. Investigation of the interaction of triethyltin with rat liver mitochondria using binding studies and Mössbauer spectroscopy. Farrow, B.G., Dawson, A.P. Eur. J. Biochem. (1978) [Pubmed]
  13. Acetylphenylhydrazine induced haemoglobin oxidation in erythrocytes studied by Mössbauer spectroscopy. Croci, S., Pedrazzi, G., Passeri, G., Piccolo, P., Ortalli, I. Biochim. Biophys. Acta (2001) [Pubmed]
  14. Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster. Kiley, P.J., Beinert, H. FEMS Microbiol. Rev. (1998) [Pubmed]
  15. Evidence for a tetranuclear iron-sulfur center in glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis. Averill, B.A., Dwivedi, A., Debrunner, P., Vollmer, S.J., Wong, J.Y., Switzer, R.L. J. Biol. Chem. (1980) [Pubmed]
  16. Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase. Kennedy, M.C., Kent, T.A., Emptage, M., Merkle, H., Beinert, H., Münck, E. J. Biol. Chem. (1984) [Pubmed]
  17. Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods. Franco, R., Moura, J.J., Moura, I., Lloyd, S.G., Huynh, B.H., Forbes, W.S., Ferreira, G.C. J. Biol. Chem. (1995) [Pubmed]
  18. Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine oxidase family of molybdenum-containing enzymes. Boll, M., Fuchs, G., Meier, C., Trautwein, A., El Kasmi, A., Ragsdale, S.W., Buchanan, G., Lowe, D.J. J. Biol. Chem. (2001) [Pubmed]
  19. Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. Abdul-Tehrani, H., Hudson, A.J., Chang, Y.S., Timms, A.R., Hawkins, C., Williams, J.M., Harrison, P.M., Guest, J.R., Andrews, S.C. J. Bacteriol. (1999) [Pubmed]
  20. Mössbauer study of beef heart cytochrome oxidase. Comparative study of the bovine enzyme and cytochrome c1aa3 from Thermus thermophilus. Kent, T.A., Young, L.J., Palmer, G., Fee, J.A., Münck, E. J. Biol. Chem. (1983) [Pubmed]
  21. Spectroscopic studies on the interaction of phosphate with uteroferrin. Doi, K., Gupta, R., Aisen, P. J. Biol. Chem. (1987) [Pubmed]
  22. EPR and Mössbauer studies of benzoyl-CoA reductase. Boll, M., Fuchs, G., Meier, C., Trautwein, A., Lowe, D.J. J. Biol. Chem. (2000) [Pubmed]
  23. Pyrogenic iron(III)-doped TiO2 nanopowders synthesized in RF thermal plasma: phase formation, defect structure, band gap, and magnetic properties. Wang, X.H., Li, J.G., Kamiyama, H., Katada, M., Ohashi, N., Moriyoshi, Y., Ishigaki, T. J. Am. Chem. Soc. (2005) [Pubmed]
  24. Pressure-induced magnetization in FeO: evidence from elasticity and Mössbauer spectroscopy. Kantor, A.P., Jacobsen, S.D., Kantor, I.Y., Dubrovinsky, L.S., McCammon, C.A., Reichmann, H.J., Goncharenko, I.N. Phys. Rev. Lett. (2004) [Pubmed]
  25. Deferoxamine-induced iron mobilization and redistribution of myocardial iron in cultured rat heart cells: studies of the chelatable iron pool by electron microscopy and Mössbauer spectroscopy. Shiloh, H., Iancu, T.C., Bauminger, E.R., Link, G., Pinson, A., Hershko, C. J. Lab. Clin. Med. (1992) [Pubmed]
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