메뉴 건너뛰기




Volumn , Issue , 2010, Pages 39-67

57Fe Mössbauer Spectroscopy in Chemistry and Biology

Author keywords

Fe M ssbauer spectroscopy in chemistry and biology material property investigation; M ssbauer spectra of paramagnetic complexes framework of spin Hamiltonian; M ssbauer spectroscopy and iron containing proteins and enzyme discovery

Indexed keywords


EID: 79951575904     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470602539.ch2     Document Type: Chapter
Times cited : (16)

References (57)
  • 1
    • 0001877970 scopus 로고
    • Iron-containing proteins and related analogs: complementary Mössbauer, EPR and magnetic-susceptibility studies
    • Trautwein, A. X.; Bill, E.; Bominaar, E. L.; Winkler, H. Iron-containing proteins and related analogs: complementary Mössbauer, EPR and magnetic-susceptibility studies. Struct. Bond. 1991, 78, 1-95.
    • (1991) Struct. Bond. , vol.78 , pp. 1-95
    • Trautwein, A.X.1    Bill, E.2    Bominaar, E.L.3    Winkler, H.4
  • 2
    • 0014743042 scopus 로고
    • Mössbauer spectroscopy of heme proteins
    • Lang, G. Mössbauer spectroscopy of heme proteins. Q. Rev. Biophys. 1970, 3(1), 1-60.
    • (1970) Q. Rev. Biophys , vol.3 , Issue.1 , pp. 1-60
    • Lang, G.1
  • 4
    • 0002822447 scopus 로고    scopus 로고
    • Aspects of 57Fe Mössbauer spectroscopy
    • Lawrence Que, J., Jr., Ed.; University Science Books: Sausalito, CA
    • Münck, E. Aspects of 57Fe Mössbauer spectroscopy. In Physical Methods in Bioinorganic Chemistry: Spectroscopy and Magnetism; Lawrence Que, J., Jr., Ed.; University Science Books: Sausalito, CA, 2000; pp 287-319.
    • (2000) Physical Methods in Bioinorganic Chemistry: Spectroscopy and Magnetism , pp. 287-319
    • Münck, E.1
  • 5
    • 0018064716 scopus 로고
    • Mössbauer spectroscopy of proteins: electron carriers
    • Fleisher, S.; Packer, L., Eds.; Academic Press: New York
    • Münck, E. Mössbauer spectroscopy of proteins: electron carriers. In Methods in Enzymology; Fleisher, S.; Packer, L., Eds.; Academic Press: New York, 1978; Vol. 54, pp 346-379.
    • (1978) Methods in Enzymology , vol.54 , pp. 346-379
    • Münck, E.1
  • 6
    • 0004214293 scopus 로고
    • Dolphin, D., Ed.; Academic Press: New York
    • Münck, E. In The Porphyrins; Dolphin, D., Ed.; Academic Press: New York, 1978; Vol. 4.
    • (1978) The Porphyrins , vol.4
    • Münck, E.1
  • 7
    • 0027330259 scopus 로고
    • Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance
    • Riordan, J. F.; Vallee, B. L., Eds.; Academic Press: New York
    • Münck, E.; Surerus, K. K.; Hendrich, M. P. Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance. In Methods in Enzymology; Riordan, J. F.; Vallee, B. L., Eds.; Academic Press: New York, 1993; Vol. 227, pp 463-479.
    • (1993) Methods in Enzymology , vol.227 , pp. 463-479
    • Münck, E.1    Surerus, K.K.2    Hendrich, M.P.3
  • 8
    • 84885541213 scopus 로고    scopus 로고
    • http://www.mossbauer.org/.
  • 9
    • 84885547336 scopus 로고    scopus 로고
    • SEE Co, Edina, MN, WMOSS software package.
  • 10
    • 0000108382 scopus 로고
    • Mössbauer and integer-spin EPR of the oxidized P-clusters of nitrogenase: POX is a non-Kramers system with a nearly degenerate ground doublet
    • Surerus, K. K.; Hendrich, M. P.; Christie, P. D.; Rottgardt, D.; Orme-Johnson, W. H.; Münck, E.Mössbauer and integer-spin EPR of the oxidized P-clusters of nitrogenase: POX is a non-Kramers system with a nearly degenerate ground doublet. J. Am. Chem. Soc. 1992, 114(22), 8579-8590.
    • (1992) J. Am. Chem. Soc , vol.114 , Issue.22 , pp. 8579-8590
    • Surerus, K.K.1    Hendrich, M.P.2    Christie, P.D.3    Rottgardt, D.4    Orme-Johnson, W.H.5    Münck, E.6
  • 12
    • 0018925363 scopus 로고
    • Mössbauer spectroscopic studies of ferric hexaquo complex in amorphous frozen solutions at weak applied magnetic fields
    • Knudsen, J.E. Mössbauer spectroscopic studies of ferric hexaquo complex in amorphous frozen solutions at weak applied magnetic fields. J. Phys. Chem. Solids 1980, 41(6), 545-550.
    • (1980) J. Phys. Chem. Solids , vol.41 , Issue.6 , pp. 545-550
    • Knudsen J.E1
  • 13
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates
    • Costas, M.; Mehn, M. P.; Jensen, M. P.; Que, L. J. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem. Rev. 2004, 104(2), 939-986.
    • (2004) Chem. Rev , vol.104 , Issue.2 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que, L.J.4
  • 14
    • 38049169173 scopus 로고    scopus 로고
    • Asynthetic precedent for the [FeIV 2(mu-O)2] diamond core proposed for methane monooxygenase intermediate Q.
    • Xue, G.;Wang, D.; De Hont, R.; Fiedler, A.T.; Shan, X.; Munck, E.; Que, L., Jr.Asynthetic precedent for the [FeIV 2(mu-O)2] diamond core proposed for methane monooxygenase intermediate Q. Proc. Natl. Acad. Sci. USA 2007, 104(52), 20713-20718.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.52 , pp. 20713-20718
    • Xue, G.1    Wang, D.2    De Hont, R.3    Fiedler, A.T.4    Shan, X.5    Munck, E.6    Que Jr., L.7
  • 15
    • 33645874512 scopus 로고    scopus 로고
    • High-valent iron complexes with tetraamido macrocyclic ligands: structures, Mössbauer spectroscopy, and DFT calculations
    • Chanda, A.; Popescu, D. L.; Tiago de Oliveira, F.; Bominaar, E. L.; Ryabov, A. D.; Münck, E.; Collins, T. J. High-valent iron complexes with tetraamido macrocyclic ligands: structures, Mössbauer spectroscopy, and DFT calculations. J. Inorg. Biochem. 2006, 100(4), 606-619.
    • (2006) J. Inorg. Biochem , vol.100 , Issue.4 , pp. 606-619
    • Chanda, A.1    Popescu, D.L.2    Tiago de Oliveira, F.3    Bominaar, E.L.4    Ryabov, A.D.5    Münck, E.6    Collins, T.J.7
  • 22
    • 31344479543 scopus 로고    scopus 로고
    • The Leeuwenhoek lecture 2000. The natural and unnatural history of methaneoxidizing bacteria
    • Dalton, H. The Leeuwenhoek lecture 2000. The natural and unnatural history of methaneoxidizing bacteria. Phil. Trans. R. Soc. Lond. B: Biol. Sci. 2005, 360(1458), 1207-1222.
    • (2005) Phil. Trans. R. Soc. Lond. B: Biol. Sci , vol.360 , Issue.1458 , pp. 1207-1222
    • Dalton, H.1
  • 23
    • 0024970671 scopus 로고
    • Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph
    • Fox, B. G.; Froland, W. A.; Dege, J. E.; Lipscomb, J. D. Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. J. Biol. Chem. 1989, 264(17), 10023-10033.
    • (1989) J. Biol. Chem , vol.264 , Issue.17 , pp. 10023-10033
    • Fox, B.G.1    Froland, W.A.2    Dege, J.E.3    Lipscomb, J.D.4
  • 24
    • 0022346556 scopus 로고
    • Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity
    • Green, J.; Dalton, H. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity. J. Biol. Chem. 1985, 260(29), 15795-15801.
    • (1985) J. Biol. Chem , vol.260 , Issue.29 , pp. 15795-15801
    • Green, J.1    Dalton, H.2
  • 25
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear nonheme iron clusters
    • Wallar, B. J.; Lipscomb, J. D. Dioxygen activation by enzymes containing binuclear nonheme iron clusters. Chem. Rev. 1996, 96(7), 2625-2657.
    • (1996) Chem. Rev , vol.96 , Issue.7 , pp. 2625-2657
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 26
    • 0035916223 scopus 로고    scopus 로고
    • Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle
    • Wallar, B. J.; Lipscomb, J. D. Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Biochemistry 2001, 40(7), 2220-2233.
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2220-2233
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 27
    • 0024278967 scopus 로고
    • Evidence for a m-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Moessbauer and EPR studies
    • Fox, B. G.; Surerus, K. K.; Münck, E.; Lipscomb, J. D. Evidence for a m-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Moessbauer and EPR studies. J. Biol. Chem. 1988, 263(22), 10553-10556.
    • (1988) J. Biol. Chem , vol.263 , Issue.22 , pp. 10553-10556
    • Fox, B.G.1    Surerus, K.K.2    Münck, E.3    Lipscomb, J.D.4
  • 29
    • 0029379564 scopus 로고
    • Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Liu, K. E.; Valentine, A. M.;Wang, D.; Huynh, B. H.; Edmondson, D. E.; Salifoglou, A.; Lippard, S. J. Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath). J. Am. Chem. Soc. 1995, 117(41), 10174-10175.
    • (1995) J. Am. Chem. Soc , vol.117 , Issue.41 , pp. 10174-10175
    • Liu, K.E.1    Valentine, A.M.2    Wang, D.3    Huynh, B.H.4    Edmondson, D.E.5    Salifoglou, A.6    Lippard, S.J.7
  • 30
    • 0001016575 scopus 로고
    • Mössbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox, B. G.; Hendrich, M. P.; Surerus, K. K.; Andersson, K. K.; Froland, W. A.; Lipscomb, J. D.; Münck, E. Mössbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b. J. Am. Chem. Soc. 1993, 115(9), 3688-3701.
    • (1993) J. Am. Chem. Soc , vol.115 , Issue.9 , pp. 3688-3701
    • Fox, B.G.1    Hendrich, M.P.2    Surerus, K.K.3    Andersson, K.K.4    Froland, W.A.5    Lipscomb, J.D.6    Münck, E.7
  • 32
  • 33
    • 0348087046 scopus 로고    scopus 로고
    • The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
    • Basu, P.; Katterle, B.; Andersson, K. K.; Dalton, H. The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 2003, 369(2), 417-427.
    • (2003) Biochem. J , vol.369 , Issue.2 , pp. 417-427
    • Basu, P.1    Katterle, B.2    Andersson, K.K.3    Dalton, H.4
  • 34
    • 0037386563 scopus 로고    scopus 로고
    • Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
    • Lieberman, R. L.; Shrestha, D. B.; Doan, P. E.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proc. Natl. Acad. Sci. USA 2003, 100(7), 3820-3825.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.7 , pp. 3820-3825
    • Lieberman, R.L.1    Shrestha, D.B.2    Doan, P.E.3    Hoffman, B.M.4    Stemmler, T.L.5    Rosenzweig, A.C.6
  • 35
    • 0032526872 scopus 로고    scopus 로고
    • Purification and properties of particulate methane monooxygenase from Methylosinus trichosporium OB3b
    • Takeguchi, M.; Miyakawa, K.; Okura, I. Purification and properties of particulate methane monooxygenase from Methylosinus trichosporium OB3b. J. Mol. Catal. A 1998, 132 (2-3), 145-153.
    • (1998) J. Mol. Catal. A , vol.132 , Issue.2-3 , pp. 145-153
    • Takeguchi, M.1    Miyakawa, K.2    Okura, I.3
  • 36
    • 0030067648 scopus 로고    scopus 로고
    • Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
    • Zahn, J. A.; DiSpirito, A. A. Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 1996, 178(4), 1018-1029.
    • (1996) J. Bacteriol , vol.178 , Issue.4 , pp. 1018-1029
    • Zahn, J.A.1    DiSpirito, A.A.2
  • 37
    • 0032478599 scopus 로고    scopus 로고
    • The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization
    • Nguyen, H. H.; Elliott, S. J.;Yip, J. H.; Chan, S. I. The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization. J. Biol. Chem. 1998, 273(14), 7957-7966.
    • (1998) J. Biol. Chem , vol.273 , Issue.14 , pp. 7957-7966
    • Nguyen, H.H.1    Elliott, S.J.2    Yip, J.H.3    Chan, S.I.4
  • 39
    • 4644230771 scopus 로고    scopus 로고
    • Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria
    • Chan, S. I.; Chen, K. H.-C.; Yu, S. S. F.; Chen, C. L.; Kuo, S. S. J. Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria. Biochemistry 2004, 43, 4421-4430.
    • (2004) Biochemistry , vol.43 , pp. 4421-4430
    • Chan, S.I.1    Chen, K.H.-C.2    Yu, S.S.F.3    Chen, C.L.4    Kuo, S.S.J.5
  • 41
    • 15044356424 scopus 로고    scopus 로고
    • Crystal structure of a membrane-bound metalloenzyme that catalyzes the biological oxidation of methane
    • Lieberman, R. L.; Rosenzweig, A. C. Crystal structure of a membrane-bound metalloenzyme that catalyzes the biological oxidation of methane. Nature 2005, 434(7030), 177-182.
    • (2005) Nature , vol.434 , Issue.7030 , pp. 177-182
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 42
    • 12644275421 scopus 로고    scopus 로고
    • X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath): Cu(I) ions and their implications
    • Nguyen, H.-H.T.; Nakagawa, K. H.; Hedman, B.; Elliott, S. J.; Lidstrom, M. E.; Hodgson, K. O.; Chan, S. I. X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath): Cu(I) ions and their implications. J. Am. Chem. Soc. 1996, 118, 12766-12776.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12766-12776
    • Nguyen, H.-H.T.1    Nakagawa, K.H.2    Hedman, B.3    Elliott, S.J.4    Lidstrom, M.E.5    Hodgson, K.O.6    Chan, S.I.7
  • 44
    • 37549052557 scopus 로고    scopus 로고
    • Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus bath: evidence for a diiron center
    • Martinho, M.; Choi, D. W.; Dispirito, A. A.; Antholine, W. E.; Semrau, J. D.; Münck, E. Mössbauer studies of the membrane-associated methane monooxygenase from Methylococcus capsulatus bath: evidence for a diiron center. J. Am. Chem. Soc. 2007, 129(51), 15783-15785.
    • (2007) J. Am. Chem. Soc , vol.129 , Issue.51 , pp. 15783-15785
    • Martinho, M.1    Choi, D.W.2    Dispirito, A.A.3    Antholine, W.E.4    Semrau, J.D.5    Münck, E.6
  • 45
    • 0025036376 scopus 로고
    • Methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox, B. G.; Froland, W. A.; Jollie, D. R.; Lipscomb, J. D. Methane monooxygenase from Methylosinus trichosporium OB3b. Methods Enzymol. 1990, 188, 191-202.
    • (1990) Methods Enzymol. , vol.188 , pp. 191-202
    • Fox, B.G.1    Froland, W.A.2    Jollie, D.R.3    Lipscomb, J.D.4
  • 46
    • 4444257275 scopus 로고    scopus 로고
    • Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase
    • Lieberman, R. L.; Rosenzweig, A. C. Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 2004, 39(3), 147-164.
    • (2004) Crit. Rev. Biochem. Mol. Biol , vol.39 , Issue.3 , pp. 147-164
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 47
    • 23944513777 scopus 로고    scopus 로고
    • Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)
    • Kitmitto, A.; Myronova, N.; Basu, P.; Dalton, H. Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 2005, 44(33), 10954-10965.
    • (2005) Biochemistry , vol.44 , Issue.33 , pp. 10954-10965
    • Kitmitto, A.1    Myronova, N.2    Basu, P.3    Dalton, H.4
  • 49
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • Beinert, H.; Holm, R. H.; Münck, E. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 1997, 277(5326), 653-659.
    • (1997) Science , vol.277 , Issue.5326 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 50
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert, H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 2000, 5(1), 2-15.
    • (2000) J. Biol. Inorg. Chem , vol.5 , Issue.1 , pp. 2-15
    • Beinert, H.1
  • 52
    • 0030544904 scopus 로고    scopus 로고
    • Synthesis, structure and magnetic properties of ferritin cores with varying composition and degrees of structural order: models for iron oxide deposits in ironoverload diseases
    • St. Pierre, T. G.; Chan, P.; Bauchspiess, K. R.; Webb, J.; Betteridge, S.; Walton, S.; Dickson, D. P. E. Synthesis, structure and magnetic properties of ferritin cores with varying composition and degrees of structural order: models for iron oxide deposits in ironoverload diseases. Coord. Chem. Rev. 1996, 151, 125-143.
    • (1996) Coord. Chem. Rev. , vol.151 , pp. 125-143
    • St. Pierre, T.G.1    Chan, P.2    Bauchspiess, K.R.3    Webb, J.4    Betteridge, S.5    Walton, S.6    Dickson, D.P.E.7
  • 53
    • 0003163924 scopus 로고
    • Mössbauer effect studies of microcrystalline materials
    • Long, G. J., Ed.; Plenum Press: New York
    • Mørup, S. Mössbauer effect studies of microcrystalline materials. In Mössbauer Spectroscopy Applied to Inorganic Chemistry; Long, G. J., Ed.; Plenum Press: New York, 1984; Vol. 2.
    • (1984) Mössbauer Spectroscopy Applied to Inorganic Chemistry , vol.2
    • Mørup, S.1
  • 54
    • 0021910561 scopus 로고
    • Electron spin resonance studies of splenic ferritin and haemosiderin
    • Weir, M.P.; Peters, T.J.; Gibson, J.F. Electron spin resonance studies of splenic ferritin and haemosiderin. Biochim. Biophys. Acta 1985, 828(3), 298-305.
    • (1985) Biochim. Biophys. Acta , vol.828 , Issue.3 , pp. 298-305
    • Weir, M.P.1    Peters, T.J.2    Gibson, J.F.3
  • 55
    • 0035743682 scopus 로고    scopus 로고
    • Ferromagnetic resonance of horse spleen ferritin: core blocking and surface ordering temperatures
    • Wajnberg, E.; El-Jaick, L.J.; Linhares, M.P.; Esquivel, D.M. Ferromagnetic resonance of horse spleen ferritin: core blocking and surface ordering temperatures. J. Magn. Reson. 2001, 153(1), 69-74.
    • (2001) J. Magn. Reson , vol.153 , Issue.1 , pp. 69-74
    • Wajnberg, E.1    El-Jaick, L.J.2    Linhares, M.P.3    Esquivel, D.M.4
  • 56
    • 51849115120 scopus 로고    scopus 로고
    • EPR and Mössbauer spectroscopic characterization of the accumulated iron in mitochondria from Yah1-depleted Saccharomyces cerevisiae
    • Miao, R.; Morales, J. G.; Martinho, M.; Stubna, A.; Lill, R.; Münck, E.; Lindahl, P. EPR and Mössbauer spectroscopic characterization of the accumulated iron in mitochondria from Yah1-depleted Saccharomyces cerevisiae. Biochemistry 2008, 47, 9888-9899.
    • (2008) Biochemistry , vol.47 , pp. 9888-9899
    • Miao, R.1    Morales, J.G.2    Martinho, M.3    Stubna, A.4    Lill, R.5    Münck, E.6    Lindahl, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.