메뉴 건너뛰기




Volumn 56, Issue 14, 2017, Pages 8147-8158

Iron L2,3-Edge X-ray Absorption and X-ray Magnetic Circular Dichroism Studies of Molecular Iron Complexes with Relevance to the FeMoco and FeVco Active Sites of Nitrogenase

Author keywords

[No Author keywords available]

Indexed keywords

BIOMIMETIC MATERIAL; COORDINATION COMPOUND; IRON DERIVATIVE; NITROGENASE;

EID: 85024398483     PISSN: 00201669     EISSN: 1520510X     Source Type: Journal    
DOI: 10.1021/acs.inorgchem.7b00852     Document Type: Article
Times cited : (36)

References (99)
  • 1
    • 77949495410 scopus 로고    scopus 로고
    • Decoding the Nitrogenase Mechanism: The Homologue Approach
    • Hu, Y. L.; Ribbe, M. W. Decoding the Nitrogenase Mechanism: The Homologue Approach Acc. Chem. Res. 2010, 43, 475-484 10.1021/ar900254x
    • (2010) Acc. Chem. Res. , vol.43 , pp. 475-484
    • Hu, Y.L.1    Ribbe, M.W.2
  • 2
    • 0001219252 scopus 로고    scopus 로고
    • Structure-function relationships of alternative nitrogenases
    • Eady, R. R. Structure-function relationships of alternative nitrogenases Chem. Rev. 1996, 96, 3013-3030 10.1021/cr950057h
    • (1996) Chem. Rev. , vol.96 , pp. 3013-3030
    • Eady, R.R.1
  • 3
    • 84925487767 scopus 로고    scopus 로고
    • Nitrogenase and homologs
    • Hu, Y. L.; Ribbe, M. W. Nitrogenase and homologs JBIC, J. Biol. Inorg. Chem. 2015, 20, 435-445 10.1007/s00775-014-1225-3
    • (2015) JBIC, J. Biol. Inorg. Chem. , vol.20 , pp. 435-445
    • Hu, Y.L.1    Ribbe, M.W.2
  • 4
    • 81555207920 scopus 로고    scopus 로고
    • X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor
    • Lancaster, K. M.; Roemelt, M.; Ettenhuber, P.; Hu, Y. L.; Ribbe, M. W.; Neese, F.; Bergmann, U.; DeBeer, S. X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor Science 2011, 334, 974-977 10.1126/science.1206445
    • (2011) Science , vol.334 , pp. 974-977
    • Lancaster, K.M.1    Roemelt, M.2    Ettenhuber, P.3    Hu, Y.L.4    Ribbe, M.W.5    Neese, F.6    Bergmann, U.7    DeBeer, S.8
  • 5
    • 84945458559 scopus 로고    scopus 로고
    • The Fe-V Cofactor of Vanadium Nitrogenase Contains an Interstitial Carbon Atom
    • Rees, J. A.; Bjornsson, R.; Schlesier, J.; Sippel, D.; Einsle, O.; DeBeer, S. The Fe-V Cofactor of Vanadium Nitrogenase Contains an Interstitial Carbon Atom Angew. Chem., Int. Ed. 2015, 54, 13249-13252 10.1002/anie.201505930
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 13249-13252
    • Rees, J.A.1    Bjornsson, R.2    Schlesier, J.3    Sippel, D.4    Einsle, O.5    DeBeer, S.6
  • 6
    • 0024286855 scopus 로고
    • The Vanadium Iron Protein of Vanadium Nitrogenase from Azotobacter-Chroococcum Contains an Iron Vanadium Cofactor
    • Smith, B. E.; Eady, R. R.; Lowe, D. J.; Gormal, C. The Vanadium Iron Protein of Vanadium Nitrogenase from Azotobacter-Chroococcum Contains an Iron Vanadium Cofactor Biochem. J. 1988, 250, 299-302 10.1042/bj2500299
    • (1988) Biochem. J. , vol.250 , pp. 299-302
    • Smith, B.E.1    Eady, R.R.2    Lowe, D.J.3    Gormal, C.4
  • 7
    • 0000530315 scopus 로고
    • The Iron Molybdenum Cofactor of Nitrogenase
    • Burgess, B. K. The Iron Molybdenum Cofactor of Nitrogenase Chem. Rev. 1990, 90, 1377-1406 10.1021/cr00106a002
    • (1990) Chem. Rev. , vol.90 , pp. 1377-1406
    • Burgess, B.K.1
  • 12
    • 80051763661 scopus 로고    scopus 로고
    • Spectroscopic Characterization of the Isolated Iron-Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN
    • Fay, A. W.; Blank, M. A.; Lee, C. C.; Hu, Y. L.; Hodgson, K. O.; Hedman, B.; Ribbe, M. W. Spectroscopic Characterization of the Isolated Iron-Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN Angew. Chem., Int. Ed. 2011, 50, 7787-7790 10.1002/anie.201102724
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 7787-7790
    • Fay, A.W.1    Blank, M.A.2    Lee, C.C.3    Hu, Y.L.4    Hodgson, K.O.5    Hedman, B.6    Ribbe, M.W.7
  • 13
    • 84939950424 scopus 로고    scopus 로고
    • The role of X-ray spectroscopy in understanding the geometric and electronic structure of nitrogenase
    • Kowalska, J.; DeBeer, S. The role of X-ray spectroscopy in understanding the geometric and electronic structure of nitrogenase Biochim. Biophys. Acta, Mol. Cell Res. 2015, 1853, 1406-1415 10.1016/j.bbamcr.2014.11.027
    • (2015) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1853 , pp. 1406-1415
    • Kowalska, J.1    DeBeer, S.2
  • 14
    • 0037189539 scopus 로고    scopus 로고
    • The FeMoco-deficient MoFe protein produced by a nifH deletion strain of Azotobacter vinelandii shows unusual P-cluster features
    • Ribbe, M. W.; Hu, Y. L.; Guo, M. L.; Schmid, B.; Burgess, B. K. The FeMoco-deficient MoFe protein produced by a nifH deletion strain of Azotobacter vinelandii shows unusual P-cluster features J. Biol. Chem. 2002, 277, 23469-23476 10.1074/jbc.M202061200
    • (2002) J. Biol. Chem. , vol.277 , pp. 23469-23476
    • Ribbe, M.W.1    Hu, Y.L.2    Guo, M.L.3    Schmid, B.4    Burgess, B.K.5
  • 18
    • 85011898487 scopus 로고    scopus 로고
    • Revisiting the Mössbauer Isomer Shifts of the FeMoco Cluster of Nitrogenase and the Cofactor Charge
    • Bjornsson, R.; Neese, F.; DeBeer, S. Revisiting the Mössbauer Isomer Shifts of the FeMoco Cluster of Nitrogenase and the Cofactor Charge Inorg. Chem. 2017, 56, 1470-1477 10.1021/acs.inorgchem.6b02540
    • (2017) Inorg. Chem. , vol.56 , pp. 1470-1477
    • Bjornsson, R.1    Neese, F.2    DeBeer, S.3
  • 20
    • 85024368611 scopus 로고    scopus 로고
    • Telser, J. American Chemical Society: Washington, DC, Chapter 20
    • Cramer, S. P. In Paramagnetic Resonance of Metallobiomolecules; Telser, J., Ed.; American Chemical Society: Washington, DC, 2003; Chapter 20, pp 358-402.
    • (2003) Paramagnetic Resonance of Metallobiomolecules , pp. 358-402
    • Cramer, S.P.1
  • 22
    • 46749086288 scopus 로고    scopus 로고
    • XMCD studies on Co and Li doped ZnO magnetic semiconductors
    • Tietze, T.; Gacic, M.; Schutz, G.; Jakob, G.; Bruck, S.; Goering, E. XMCD studies on Co and Li doped ZnO magnetic semiconductors New J. Phys. 2008, 10, 055009 10.1088/1367-2630/10/5/055009
    • (2008) New J. Phys. , vol.10 , pp. 055009
    • Tietze, T.1    Gacic, M.2    Schutz, G.3    Jakob, G.4    Bruck, S.5    Goering, E.6
  • 24
    • 84994832061 scopus 로고    scopus 로고
    • Magnetic properties of supported metal atoms and clusters
    • Martins, M.; Wurth, W. Magnetic properties of supported metal atoms and clusters J. Phys.: Condens. Matter 2016, 28, 503002 10.1088/0953-8984/28/50/503002
    • (2016) J. Phys.: Condens. Matter , vol.28 , pp. 503002
    • Martins, M.1    Wurth, W.2
  • 33
    • 0002080469 scopus 로고
    • X-ray magnetic circular dichroism spectroscopy of transition metal thin films
    • Stohr, J. X-ray magnetic circular dichroism spectroscopy of transition metal thin films J. Electron Spectrosc. Relat. Phenom. 1995, 75, 253-272 10.1016/0368-2048(95)02537-5
    • (1995) J. Electron Spectrosc. Relat. Phenom. , vol.75 , pp. 253-272
    • Stohr, J.1
  • 35
    • 11144340356 scopus 로고    scopus 로고
    • Recent advances in x-ray absorption spectroscopy
    • Wende, H. Recent advances in x-ray absorption spectroscopy Rep. Prog. Phys. 2004, 67, 2105-2181 10.1088/0034-4885/67/12/R01
    • (2004) Rep. Prog. Phys. , vol.67 , pp. 2105-2181
    • Wende, H.1
  • 36
    • 28944434100 scopus 로고    scopus 로고
    • X-ray magnetic circular dichroism on Pt L-edges in Co-based materials
    • Poulopoulos, P. X-ray magnetic circular dichroism on Pt L-edges in Co-based materials Int. J. Mod. Phys. B 2005, 19, 4517-4523 10.1142/S0217979205032905
    • (2005) Int. J. Mod. Phys. B , vol.19 , pp. 4517-4523
    • Poulopoulos, P.1
  • 37
    • 0031606685 scopus 로고    scopus 로고
    • Magnetic properties of transition metal multilayers studied with X-ray magnetic circular dichroism spectroscopy
    • Stohr, J.; Nakajima, R. Magnetic properties of transition metal multilayers studied with X-ray magnetic circular dichroism spectroscopy IBM J. Res. Dev. 1998, 42, 73-88 10.1147/rd.421.0073
    • (1998) IBM J. Res. Dev. , vol.42 , pp. 73-88
    • Stohr, J.1    Nakajima, R.2
  • 38
    • 44349096592 scopus 로고    scopus 로고
    • Cation site occupancy of biogenic magnetite compared to polygenic ferrite spinels determined by X-ray magnetic circular dichroism
    • Coker, V. S.; Pearce, C. I.; Lang, C.; van der Laan, G.; Pattrick, R. A. D.; Telling, N. D.; Schuler, D.; Arenholz, E.; Lloyd, J. R. Cation site occupancy of biogenic magnetite compared to polygenic ferrite spinels determined by X-ray magnetic circular dichroism Eur. J. Mineral. 2007, 19, 707-716 10.1127/0935-1221/2007/0019-1758
    • (2007) Eur. J. Mineral. , vol.19 , pp. 707-716
    • Coker, V.S.1    Pearce, C.I.2    Lang, C.3    Van Der Laan, G.4    Pattrick, R.A.D.5    Telling, N.D.6    Schuler, D.7    Arenholz, E.8    Lloyd, J.R.9
  • 39
    • 84856797869 scopus 로고    scopus 로고
    • Examining the chemistry and magnetism of magnetotactic bacterium Candidatus Magnetovibrio blakemorei strain MV-1 using scanning transmission X-ray microscopy
    • Kalirai, S. S.; Lam, K. P.; Bazylinski, D. A.; Lins, U.; Hitchcock, A. P. Examining the chemistry and magnetism of magnetotactic bacterium Candidatus Magnetovibrio blakemorei strain MV-1 using scanning transmission X-ray microscopy Chem. Geol. 2012, 300-301, 14-23 10.1016/j.chemgeo.2012.01.005
    • (2012) Chem. Geol. , vol.300 , pp. 14-23
    • Kalirai, S.S.1    Lam, K.P.2    Bazylinski, D.A.3    Lins, U.4    Hitchcock, A.P.5
  • 43
    • 84872196535 scopus 로고    scopus 로고
    • Anomalous Magnetic Orientations of Magnetosome Chains in a Magnetotactic Bacterium: Magnetovibrio blakemorei Strain MV-1
    • Kalirai, S. S.; Bazylinski, D. A.; Hitchcock, A. P. Anomalous Magnetic Orientations of Magnetosome Chains in a Magnetotactic Bacterium: Magnetovibrio blakemorei Strain MV-1 PLoS One 2013, 8, e53368 10.1371/journal.pone.0053368
    • (2013) PLoS One , vol.8 , pp. e53368
    • Kalirai, S.S.1    Bazylinski, D.A.2    Hitchcock, A.P.3
  • 46
    • 0029639173 scopus 로고
    • L-Edge X-Ray-Absorption and X-Ray Magnetic Circular-Dichroism of Oxygen-Bridged Dinuclear Iron Complexes
    • Peng, G.; van Elp, J.; Jang, H.; Que, L.; Armstrong, W. H.; Cramer, S. P. L-Edge X-Ray-Absorption and X-Ray Magnetic Circular-Dichroism of Oxygen-Bridged Dinuclear Iron Complexes J. Am. Chem. Soc. 1995, 117, 2515-2519 10.1021/ja00114a014
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2515-2519
    • Peng, G.1    Van Elp, J.2    Jang, H.3    Que, L.4    Armstrong, W.H.5    Cramer, S.P.6
  • 47
    • 0036493982 scopus 로고    scopus 로고
    • Requirements for x-ray magnetic circular dichroism on paramagnetic biological systems and model compounds
    • Funk, T.; Friedrich, S.; Young, A.; Arenholz, E.; Cramer, S. P. Requirements for x-ray magnetic circular dichroism on paramagnetic biological systems and model compounds Rev. Sci. Instrum. 2002, 73, 1649-1651 10.1063/1.1445829
    • (2002) Rev. Sci. Instrum. , vol.73 , pp. 1649-1651
    • Funk, T.1    Friedrich, S.2    Young, A.3    Arenholz, E.4    Cramer, S.P.5
  • 52
    • 11144250845 scopus 로고    scopus 로고
    • X-ray magnetic circular dichroism - A high energy probe of magnetic properties Coordin
    • Funk, T.; Deb, A.; George, S. J.; Wang, H. X.; Cramer, S. P. X-ray magnetic circular dichroism-a high energy probe of magnetic properties Coordin Coord. Chem. Rev. 2005, 249, 3-30 10.1016/j.ccr.2004.05.017
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 3-30
    • Funk, T.1    Deb, A.2    George, S.J.3    Wang, H.X.4    Cramer, S.P.5
  • 59
    • 33845374418 scopus 로고
    • Assembly of Vanadium Iron Sulfur Cubane Clusters from Mononuclear and Linear Trinuclear Reactants
    • Kovacs, J. A.; Holm, R. H. Assembly of Vanadium Iron Sulfur Cubane Clusters from Mononuclear and Linear Trinuclear Reactants J. Am. Chem. Soc. 1986, 108, 340-341 10.1021/ja00262a050
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 340-341
    • Kovacs, J.A.1    Holm, R.H.2
  • 60
    • 0000204266 scopus 로고
    • X-Ray Absorption of Azotobacter-Vinelandii Vanadium Nitrogenase
    • George, G. N.; Coyle, C. L.; Hales, B. J.; Cramer, S. P. X-Ray Absorption of Azotobacter-Vinelandii Vanadium Nitrogenase J. Am. Chem. Soc. 1988, 110, 4057-4059 10.1021/ja00220a066
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4057-4059
    • George, G.N.1    Coyle, C.L.2    Hales, B.J.3    Cramer, S.P.4
  • 61
    • 0024969858 scopus 로고
    • Vanadium K-Edge X-Ray-Absorption Spectroscopy of the Functioning and Thionine-Oxidized Forms of the Vfe-Protein of the Vanadium Nitrogenase from Azotobacter-Chroococcum
    • Arber, J. M.; Dobson, B. R.; Eady, R. R.; Hasnain, S. S.; Garner, C. D.; Matsushita, T.; Nomura, M.; Smith, B. E. Vanadium K-Edge X-Ray-Absorption Spectroscopy of the Functioning and Thionine-Oxidized Forms of the Vfe-Protein of the Vanadium Nitrogenase from Azotobacter-Chroococcum Biochem. J. 1989, 258, 733-737 10.1042/bj2580733
    • (1989) Biochem. J. , vol.258 , pp. 733-737
    • Arber, J.M.1    Dobson, B.R.2    Eady, R.R.3    Hasnain, S.S.4    Garner, C.D.5    Matsushita, T.6    Nomura, M.7    Smith, B.E.8
  • 63
    • 0037169661 scopus 로고    scopus 로고
    • 4 clusters (M = Mo, V) trigonally symmetrized with hydrotris(pyrazolyl)borate(1-) and tris(pyrazolyl)methanesulfonate(1-) capping ligands
    • 4 clusters (M = Mo, V) trigonally symmetrized with hydrotris(pyrazolyl)borate(1-) and tris(pyrazolyl)methanesulfonate(1-) capping ligands Inorg. Chem. 2002, 41, 958-966 10.1021/ic011106d
    • (2002) Inorg. Chem. , vol.41 , pp. 958-966
    • Fomitchev, D.V.1    McLauchlan, C.C.2    Holm, R.H.3
  • 65
    • 0001324712 scopus 로고
    • 2- and Oxo Sulfido Ligand Substitution by Use of Silylsulfide Reagents
    • 2- and Oxo Sulfido Ligand Substitution by Use of Silylsulfide Reagents Inorg. Chem. 1983, 22, 3809-3812 10.1021/ic00167a027
    • (1983) Inorg. Chem. , vol.22 , pp. 3809-3812
    • Do, Y.1    Simhon, E.D.2    Holm, R.H.3
  • 66
    • 33845555757 scopus 로고
    • Synthetic Models for the Iron Sulfur Protein Rubredoxin - Synthesis, Structure, and Properties of a Highly Symmetric Iron(III) Tetrathiolate Anion
    • Millar, M.; Lee, J. F.; Koch, S. A.; Fikar, R. Synthetic Models for the Iron Sulfur Protein Rubredoxin-Synthesis, Structure, and Properties of a Highly Symmetric Iron(Iii) Tetrathiolate Anion Inorg. Chem. 1982, 21, 4105-4106 10.1021/ic00141a048
    • (1982) Inorg. Chem. , vol.21 , pp. 4105-4106
    • Millar, M.1    Lee, J.F.2    Koch, S.A.3    Fikar, R.4
  • 68
    • 0020766701 scopus 로고
    • 2-
    • 4-, Examples of the Newest Types of Fe-S-Sr Clusters
    • 4-, Examples of the Newest Types of Fe-S-Sr Clusters J. Am. Chem. Soc. 1983, 105, 3905-3913 10.1021/ja00350a028
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3905-3913
    • Hagen, K.S.1    Watson, A.D.2    Holm, R.H.3
  • 69
    • 80052860281 scopus 로고    scopus 로고
    • The Complete Characterization of a Reduced Biomimetic [2Fe-2S] Cluster
    • Albers, A.; Demeshko, S.; Dechert, S.; Bill, E.; Bothe, E.; Meyer, F. The Complete Characterization of a Reduced Biomimetic [2Fe-2S] Cluster Angew. Chem., Int. Ed. 2011, 50, 9191-9194 10.1002/anie.201100727
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 9191-9194
    • Albers, A.1    Demeshko, S.2    Dechert, S.3    Bill, E.4    Bothe, E.5    Meyer, F.6
  • 74
    • 1842554767 scopus 로고    scopus 로고
    • Soft x-ray magnetic circular dichroism at 2 K: A tool in biological inorganic chemistry
    • Funk, T.; Friedrich, S.; Young, A. T.; Arenholz, E.; Delano, R.; Cramer, S. P. Soft x-ray magnetic circular dichroism at 2 K: A tool in biological inorganic chemistry Rev. Sci. Instrum. 2004, 75, 756-759 10.1063/1.1645635
    • (2004) Rev. Sci. Instrum. , vol.75 , pp. 756-759
    • Funk, T.1    Friedrich, S.2    Young, A.T.3    Arenholz, E.4    Delano, R.5    Cramer, S.P.6
  • 75
    • 84919776900 scopus 로고    scopus 로고
    • A close look at dose: Toward L-edge XAS spectral uniformity, dose quantification and prediction of metal ion photoreduction
    • van Schooneveld, M. M.; DeBeer, S. A close look at dose: Toward L-edge XAS spectral uniformity, dose quantification and prediction of metal ion photoreduction J. Electron Spectrosc. Relat. Phenom. 2015, 198, 31-56 10.1016/j.elspec.2014.12.001
    • (2015) J. Electron Spectrosc. Relat. Phenom. , vol.198 , pp. 31-56
    • Van Schooneveld, M.M.1    DeBeer, S.2
  • 76
    • 73449098906 scopus 로고    scopus 로고
    • Blueprint XAS: A Matlab-based toolbox for the fitting and analysis of XAS spectra
    • Delgado-Jaime, M. U.; Mewis, C. P.; Kennepohl, P. Blueprint XAS: a Matlab-based toolbox for the fitting and analysis of XAS spectra J. Synchrotron Radiat. 2010, 17, 132-137 10.1107/S0909049509046561
    • (2010) J. Synchrotron Radiat. , vol.17 , pp. 132-137
    • Delgado-Jaime, M.U.1    Mewis, C.P.2    Kennepohl, P.3
  • 78
  • 81
    • 44349161512 scopus 로고    scopus 로고
    • Core Level Spectroscopy of Solids Introduction
    • de Groot, F.; Kotani, A. Core Level Spectroscopy of Solids Introduction Adv. Condens Mat Sci. 2008, 6, 512 10.1201/9781420008425
    • (2008) Adv. Condens Mat Sci. , vol.6 , pp. 512
    • De Groot, F.1    Kotani, A.2
  • 82
    • 8244230321 scopus 로고
    • 2p X-Ray Absorption of 3d Transition-Metal Compounds - An Atomic Multiplet Description Including the Crystal-Field
    • de Groot, F. M. F.; Fuggle, J. C.; Thole, B. T.; Sawatzky, G. A. 2p X-Ray Absorption of 3d Transition-Metal Compounds-an Atomic Multiplet Description Including the Crystal-Field Phys. Rev. B: Condens. Matter Mater. Phys. 1990, 42, 5459-5468 10.1103/PhysRevB.42.5459
    • (1990) Phys. Rev. B: Condens. Matter Mater. Phys. , vol.42 , pp. 5459-5468
    • De Groot, F.M.F.1    Fuggle, J.C.2    Thole, B.T.3    Sawatzky, G.A.4
  • 83
    • 0000792384 scopus 로고
    • Spin-Mixed Ground-State of Fe Phthalocyanine and the Temperature-Dependent Branching Ratio in X-Ray Absorption-Spectroscopy
    • Thole, B. T.; van der Laan, G.; Butler, P. H. Spin-Mixed Ground-State of Fe Phthalocyanine and the Temperature-Dependent Branching Ratio in X-Ray Absorption-Spectroscopy Chem. Phys. Lett. 1988, 149, 295-299 10.1016/0009-2614(88)85029-2
    • (1988) Chem. Phys. Lett. , vol.149 , pp. 295-299
    • Thole, B.T.1    Van Der Laan, G.2    Butler, P.H.3
  • 84
    • 77955923315 scopus 로고    scopus 로고
    • The CTM4XAS program for EELS and XAS spectral shape analysis of transition metal L edges
    • Stavitski, E.; de Groot, F. M. F. The CTM4XAS program for EELS and XAS spectral shape analysis of transition metal L edges Micron 2010, 41, 687-694 10.1016/j.micron.2010.06.005
    • (2010) Micron , vol.41 , pp. 687-694
    • Stavitski, E.1    De Groot, F.M.F.2
  • 85
    • 0034816325 scopus 로고    scopus 로고
    • A quantitative description of the ground-state wave function of Cu-A by X-ray absorption spectroscopy: Comparison to plastocyanin and relevance to electron transfer
    • DeBeer George, S.; Metz, M.; Szilagyi, R. K.; Wang, H. X.; Cramer, S. P.; Lu, Y.; Tolman, W. B.; Hedman, B.; Hodgson, K. O.; Solomon, E. I. A quantitative description of the ground-state wave function of Cu-A by X-ray absorption spectroscopy: Comparison to plastocyanin and relevance to electron transfer J. Am. Chem. Soc. 2001, 123, 5757-5767 10.1021/ja004109i
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5757-5767
    • DeBeer George, S.1    Metz, M.2    Szilagyi, R.K.3    Wang, H.X.4    Cramer, S.P.5    Lu, Y.6    Tolman, W.B.7    Hedman, B.8    Hodgson, K.O.9    Solomon, E.I.10
  • 86
    • 0142072588 scopus 로고    scopus 로고
    • L-edge X-ray absorption spectroscopy of non-heme iron sites: Experimental determination of differential orbital covalency
    • Wasinger, E. C.; de Groot, F. M. F.; Hedman, B.; Hodgson, K. O.; Solomon, E. I. L-edge X-ray absorption spectroscopy of non-heme iron sites: Experimental determination of differential orbital covalency J. Am. Chem. Soc. 2003, 125, 12894-12906 10.1021/ja034634s
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12894-12906
    • Wasinger, E.C.1    De Groot, F.M.F.2    Hedman, B.3    Hodgson, K.O.4    Solomon, E.I.5
  • 88
    • 84889070574 scopus 로고    scopus 로고
    • L-edge X-ray absorption study of mononuclear vanadium complexes and spectral predictions using a restricted open shell configuration interaction ansatz
    • Maganas, D.; Roemelt, M.; Weyhermuller, T.; Blume, R.; Havecker, M.; Knop-Gericke, A.; DeBeer, S.; Schlogl, R.; Neese, F. L-edge X-ray absorption study of mononuclear vanadium complexes and spectral predictions using a restricted open shell configuration interaction ansatz Phys. Chem. Chem. Phys. 2014, 16, 264-276 10.1039/C3CP52711E
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 264-276
    • Maganas, D.1    Roemelt, M.2    Weyhermuller, T.3    Blume, R.4    Havecker, M.5    Knop-Gericke, A.6    DeBeer, S.7    Schlogl, R.8    Neese, F.9
  • 91
    • 0007250951 scopus 로고    scopus 로고
    • Bioinorganic applications of X-ray multiplets - The impact of Theo Thole's work
    • Cramer, S. P.; Ralston, C. Y.; Wang, H. X.; Bryant, C. Bioinorganic applications of X-ray multiplets-The impact of Theo Thole's work J. Electron Spectrosc. Relat. Phenom. 1997, 86, 175-183 10.1016/S0368-2048(97)00064-9
    • (1997) J. Electron Spectrosc. Relat. Phenom. , vol.86 , pp. 175-183
    • Cramer, S.P.1    Ralston, C.Y.2    Wang, H.X.3    Bryant, C.4
  • 92
    • 84879341412 scopus 로고    scopus 로고
    • A combined DFT and restricted open-shell configuration interaction method including spin-orbit coupling: Application to transition metal L-edge X-ray absorption spectroscopy
    • Roemelt, M.; Maganas, D.; DeBeer, S.; Neese, F. A combined DFT and restricted open-shell configuration interaction method including spin-orbit coupling: Application to transition metal L-edge X-ray absorption spectroscopy J. Chem. Phys. 2013, 138, 204101 10.1063/1.4804607
    • (2013) J. Chem. Phys. , vol.138 , pp. 204101
    • Roemelt, M.1    Maganas, D.2    DeBeer, S.3    Neese, F.4
  • 99
    • 84865706473 scopus 로고    scopus 로고
    • On the origin of dips in total fluorescence yield X-ray absorption spectra: Partial and inverse partial fluorescence yield at the L-edge of cobalt aqueous solution
    • Soldatov, M. A.; Lange, K. M.; Gotz, M. D.; Engel, N.; Golnak, R.; Kothe, A.; Aziz, E. F. On the origin of dips in total fluorescence yield X-ray absorption spectra: Partial and inverse partial fluorescence yield at the L-edge of cobalt aqueous solution Chem. Phys. Lett. 2012, 546, 164-167 10.1016/j.cplett.2012.07.067
    • (2012) Chem. Phys. Lett. , vol.546 , pp. 164-167
    • Soldatov, M.A.1    Lange, K.M.2    Gotz, M.D.3    Engel, N.4    Golnak, R.5    Kothe, A.6    Aziz, E.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.