The Experts below are selected from a list of 43743 Experts worldwide ranked by ideXlab platform
Sp Cramer - One of the best experts on this subject based on the ideXlab platform.
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l edge x ray Absorption Spectroscopy of pyrococcus furiosus rubredoxin
Journal of the American Chemical Society, 1992Co-Authors: Sj George, J Vanelp, Jb Park, B G Searle, Fmf Degroot, J C Fuggle, Michael W W Adams, C.t. Chen, Sp CramerAbstract:X-Ray Absorption Spectroscopy has been used to probe the frozen solution structure of the metal site in Pyrococcus furiosus rubredoxin in the native, iron-containing protein and in zinc- and mercury-substituted proteins. For all samples studied, the spectra have been interpreted in terms of a single shell of coordinated sulfur, with approximately tetrahedral coordination. For the native protein we obtain Fe-S bond-lengths of 2.29 and 2.33 A for oxidized and reduced proteins, respectively. These values are in excellent agreement with those previously obtained from X-Ray crystallography. The metal-substituted rubredoxins possess metal-sulfur bond lengths of 2.34 and 2.54 A for the zinc- and mercury-substituted proteins, respectively.
C.t. Chen - One of the best experts on this subject based on the ideXlab platform.
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X-Ray Absorption Spectroscopy OF PRXY1-XBA2CU3O7-Y SINGLE CRYSTALS
Journal of Low Temperature Physics, 1996Co-Authors: Mariann Merz, Jaime Fink, N Nucker, E Pellegrin, M Knupfer, M Kielwein, Mark S. Golden, Simon Schüppler, C.t. Chen, V. ChakarianAbstract:Substituting Y in orthorhombic (Y,RE)Ba2Cu3O7 by arty rare-earth element RE has generally little effect on the superconducting properties, For RE = Pr, however, superconductivity is completely suppressed. To elucidate this effect we have studied the unoccupied electronic structure of PrxY1-xBa2Cu3O7-y (x = 0.0, 0.4, 0.8) by polarization-dependent Ols X-Ray Absorption Spectroscopy on detwinned single crystals. Along with the comparison of undoped (y approximate to 0.9) to the doped materials (y approximate to 0.1), this allows a test of the current theoretical explanations for the suppression of super- conductivity, While we can rule out models involving hole filling or charge transfer from planes to chains our data is consistent with approaches based on Pr4f-O2p(pi) hybridization. [References: 16]
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Recent Advances in Soft-X-Ray Absorption Spectroscopy
Japanese Journal of Applied Physics, 1993Co-Authors: C.t. ChenAbstract:X-Ray Absorption Spectroscopy in the "soft" region has achieved major progress recently. High resolution soft-X-Rays with a high degree of linear or circular polarization can now be routinely produced, and high sensitivity soft-X-Ray fluorescence detectors are available. Soft-X-Ray Absorption experiments, recently conducted at the Dragon beamline, are utilized to demonstrate the information that can be obtained on the electronic and magnetic structure of matter, emphasizing the new scientific opportunities offered by these spectroscopic advances.
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l edge x ray Absorption Spectroscopy of pyrococcus furiosus rubredoxin
Journal of the American Chemical Society, 1992Co-Authors: Sj George, J Vanelp, Jb Park, B G Searle, Fmf Degroot, J C Fuggle, Michael W W Adams, C.t. Chen, Sp CramerAbstract:X-Ray Absorption Spectroscopy has been used to probe the frozen solution structure of the metal site in Pyrococcus furiosus rubredoxin in the native, iron-containing protein and in zinc- and mercury-substituted proteins. For all samples studied, the spectra have been interpreted in terms of a single shell of coordinated sulfur, with approximately tetrahedral coordination. For the native protein we obtain Fe-S bond-lengths of 2.29 and 2.33 A for oxidized and reduced proteins, respectively. These values are in excellent agreement with those previously obtained from X-Ray crystallography. The metal-substituted rubredoxins possess metal-sulfur bond lengths of 2.34 and 2.54 A for the zinc- and mercury-substituted proteins, respectively.
Michael W W Adams - One of the best experts on this subject based on the ideXlab platform.
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X-Ray Absorption Spectroscopy of Pyrococcus furiosus rubredoxin
Journal of Biological Inorganic Chemistry, 1996Co-Authors: Graham N. George, Zhi Hao Zhou, Ingrid J. Pickering, Roger C. Prince, Michael W W AdamsAbstract:X-Ray Absorption Spectroscopy has been used to probe the frozen solution structure of the metal site in Pyrococcus furiosus rubredoxin in the native, iron-containing protein and in zinc- and mercury-substituted proteins. For all samples studied, the spectra have been interpreted in terms of a single shell of coordinated sulfur, with approximately tetrahedral coordination. For the native protein we obtain Fe-S bond-lengths of 2.29 and 2.33 A for oxidized and reduced proteins, respectively. These values are in excellent agreement with those previously obtained from X-Ray crystallography. The metal-substituted rubredoxins possess metal-sulfur bond lengths of 2.34 and 2.54 A for the zinc- and mercury-substituted proteins, respectively.
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l edge x ray Absorption Spectroscopy of pyrococcus furiosus rubredoxin
Journal of the American Chemical Society, 1992Co-Authors: Sj George, J Vanelp, Jb Park, B G Searle, Fmf Degroot, J C Fuggle, Michael W W Adams, C.t. Chen, Sp CramerAbstract:X-Ray Absorption Spectroscopy has been used to probe the frozen solution structure of the metal site in Pyrococcus furiosus rubredoxin in the native, iron-containing protein and in zinc- and mercury-substituted proteins. For all samples studied, the spectra have been interpreted in terms of a single shell of coordinated sulfur, with approximately tetrahedral coordination. For the native protein we obtain Fe-S bond-lengths of 2.29 and 2.33 A for oxidized and reduced proteins, respectively. These values are in excellent agreement with those previously obtained from X-Ray crystallography. The metal-substituted rubredoxins possess metal-sulfur bond lengths of 2.34 and 2.54 A for the zinc- and mercury-substituted proteins, respectively.
Sj George - One of the best experts on this subject based on the ideXlab platform.
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l edge x ray Absorption Spectroscopy of pyrococcus furiosus rubredoxin
Journal of the American Chemical Society, 1992Co-Authors: Sj George, J Vanelp, Jb Park, B G Searle, Fmf Degroot, J C Fuggle, Michael W W Adams, C.t. Chen, Sp CramerAbstract:X-Ray Absorption Spectroscopy has been used to probe the frozen solution structure of the metal site in Pyrococcus furiosus rubredoxin in the native, iron-containing protein and in zinc- and mercury-substituted proteins. For all samples studied, the spectra have been interpreted in terms of a single shell of coordinated sulfur, with approximately tetrahedral coordination. For the native protein we obtain Fe-S bond-lengths of 2.29 and 2.33 A for oxidized and reduced proteins, respectively. These values are in excellent agreement with those previously obtained from X-Ray crystallography. The metal-substituted rubredoxins possess metal-sulfur bond lengths of 2.34 and 2.54 A for the zinc- and mercury-substituted proteins, respectively.
Gaetano Granozzi - One of the best experts on this subject based on the ideXlab platform.
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high resolution photoemission and x ray Absorption Spectroscopy of a lepidocrocite like tio2 nanosheet on pt 110 1 2
Journal of Chemical Physics, 2011Co-Authors: L. E. Walle, Anders Sandell, Anne Borg, Stefano Agnoli, I H Svenum, Luca Artiglia, P Kruger, Gaetano GranozziAbstract:The electronic structure of TiO(2) nanosheets on the Pt(110)-(1 x 2) surface has been investigated by using high resolution photoemission Spectroscopy and X-Ray Absorption Spectroscopy (XAS). The T ...
