Applications of X-ray absorption spectroscopy and low temperature XMCD to metalloproteins

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The author has used the extended X-ray absorption fine structure (EXAFS) and ultra-low temperature X-ray magnetic circular dichroism (XMCD) to study the environments of the metal sites in metalloproteins. EXAFS has been used to study the Zn site in spinach carbonic anhydrase. The EXAFS, in parallel with site directed mutagenesis studies, indicate that the active site Zn is in a cys-cys-his-H{sub 2}O environment, very different from the mammalian carbonic anhydrase active site. Nitrogenase, the primary enzyme in biological nitrogen fixation, contains two complex metal clusters of unique structure. EXAFS studies at the Fe and Mo K-edges of nitrogenase solutions and ... continued below

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249 p.

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Christiansen, J. H. January 1996.

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  • Christiansen, J. H. Lawrence Berkeley National Lab., CA (United States). Energy and Environment Div.

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Description

The author has used the extended X-ray absorption fine structure (EXAFS) and ultra-low temperature X-ray magnetic circular dichroism (XMCD) to study the environments of the metal sites in metalloproteins. EXAFS has been used to study the Zn site in spinach carbonic anhydrase. The EXAFS, in parallel with site directed mutagenesis studies, indicate that the active site Zn is in a cys-cys-his-H{sub 2}O environment, very different from the mammalian carbonic anhydrase active site. Nitrogenase, the primary enzyme in biological nitrogen fixation, contains two complex metal clusters of unique structure. EXAFS studies at the Fe and Mo K-edges of nitrogenase solutions and crystals yielded information about the various metal-metal distances in these two clusters. The author assigned 4 Fe and 3 Mo interactions >4 {angstrom}. Single crystal Mo K-edge EXAFS then found a very long Fe-Fe distance of {approximately}5.1 {angstrom}. These distances were then used to further refine the proposed crystallographic models to their highest accuracy yet. Studies were carried further by examining nitrogenas in oxidized and reduced forms--states for which there is no crystallographic information. Small structural changes were observed and an EXAFS model was put forth that attempts to deconvolute the EXAFS distances of the two metal clusters. Nitrogenase Apo I, a genetic mutant of nitrogenase which is though to contain only one of the two different metal clusters, was also examined using EXAFS. These studies showed results consistent with current models, yet the metal clusters were very disordered. Finally, ultra-low temperature methods were used to further the development of XMCD as a technique for studying biological systems. Experiments were performed on the copper in plastocyanin. Data was collected that definitively proves that the sample surface was at 0.55 {+-} 0.05 K. This result opens the door to further study of more complex biological metal clusters.

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249 p.

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OSTI as DE96013149

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  • Other Information: TH: Thesis (Ph.D.)

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  • Other: DE96013149
  • Report No.: LBL--38410
  • Grant Number: AC03-76SF00098
  • DOI: 10.2172/266644 | External Link
  • Office of Scientific & Technical Information Report Number: 266644
  • Archival Resource Key: ark:/67531/metadc672482

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Office of Scientific & Technical Information Technical Reports

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  • January 1996

Added to The UNT Digital Library

  • June 29, 2015, 9:42 p.m.

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  • Nov. 18, 2015, 6:30 p.m.

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Christiansen, J. H. Applications of X-ray absorption spectroscopy and low temperature XMCD to metalloproteins, report, January 1996; California. (digital.library.unt.edu/ark:/67531/metadc672482/: accessed December 13, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.