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  • 2000-2004  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Iron and copper K-edge XAS study of serotransferrin and ovotransferrin (2001)
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 8 (2001), S. 196-198 
    Details
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The active metal site structure of transferrin with iron and copper atoms is investigated using metal K-XANES. Theoretical analysis of experimental data has been performed on the basis of full multiple-scattering theory. This approach made it possible to study the origin of XANES fine details and to investigate the local structure around active metal sites. A deep insight into the local structure and electronic subsystem of Fe, Cu transferrins is obtained. For example, in the case of Cu substitution of Fe in the active centre, the best fit of theoretical spectra to experiment has been obtained for distances 3% smaller between the Cu atom and the nearest neighbours.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0909049500016307
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    MXAN : a new software procedure to perform geometrical fitting of experimental XANES spectra (2001)
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 8 (2001), S. 267-269 
    Details
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A new software procedure, MXAN, to fit experimental XANES spectra is presented here. The method is based on the comparison between the experimental spectrum and several theoretical calculations generated by changing the relevant geometrical parameter of the site around the absorbing atom. The x-ray photoabsorption cross section is calculated using the general multiple-scattering scheme, utilizing a complex Hedin-Lunqvist energy-dependent potential to describe the exchange correlation interaction. Our method has been applied to the study of geometrical environment of the tetrahedral zinc site of the protein superoxide dismutase (SOD). The experimental Zn K-edge XANES spectrum has been fitted in the space of the first shell coordination parameters (ligand distances and angles) following the behavior of the chi-square as a function of the local distortion from the starting crystallographic structure. The recovered structure is found to be independent on the starting conditions, showing the theoretical uniqueness of the structural solution. Strengths and limitations of the application to real systems are also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0909049500015338
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Comparative XANES study of serotransferrin and ovotransferrin at Cu K-edge: evidence of interactions among the metal sites (2000)
    Springer
    BioMetals 13 (2000), S. 217-222 
    Details
    ISSN: 1572-8773
    Keywords: copper site ; synchrotron radiation ; transferrins ; X-ray spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The Cu site structure of human serotransferrin and hen ovotransferrin using XANES spectroscopy has been investigated. Although the transferrin family proteins have been extensively studied, the results reported herein are the first concerning the structure of the metal site in C-terminal and N-terminal in the whole protein. Our structural data show that these proteins differ with regard to the independence of the two binding sites and the geometry of copper coordination, ranging from a poorly to a significantly distorted octahedron.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009211820077
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    Paper (German National Licenses)
    Fulltext
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