European Biophysics Journal

, Volume 24, Issue 4, pp 243–250 | Cite as

EXAFS investigation of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii

  • C. Scherk
  • M. Schmidt
  • H. -F. Nolting
  • B. Meier
  • F. Parak
Article
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Accepted:

Abstract

The local structure of the iron site in ferric superoxide dismutase from P. shermanii was analyzed by X-ray absorption spectroscopy. The metal-ligand cluster of the enzyme is found to be similar to the crystallographically investigated ferric superoxide dismutase from E. coli. At pH 6.4 the enzyme is five-fold coordinated with three histidines, an aspartate and a water molecule. The average bond lengths between the metal and the histidines are about 2.10 Å, between metal and aspartate they are about 1.86 Å and between metal and water 1.96 Å. With an increase in pH a change in the coordination number from five to six is observed both in pre-edge peak and EXAFS spectra analysis. However, the bond lengths of the ligands do not change dramatically, they are conserved for the aspartate and increase slightly to 2.13 Å for the average metal - histidine distance at pH 9.3. The observation of the increase in coordination number is correlated with a decrease in enzymatic activity which occurs in the high pH range. The zinc EXAFS spectra of P. shermanii superoxide dismutase have shown that zinc can be incorporated in the active center instead of the iron.

Key words

Iron superoxide dismutase SOD X-ray absorption XAS Extended X-ray absorption fine structure EXAFS P. shermanii E. coli Metalloproteins 
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Copyright information

© Springer-Verlag 1996

Authors and Affiliations

  • C. Scherk
    • 1
  • M. Schmidt
    • 1
  • H. -F. Nolting
    • 3
  • B. Meier
    • 2
  • F. Parak
    • 1
  1. 1.Fakultät für Physik E17Technische Universität MünchenGarchingGermany
  2. 2.Tierärztliche Hochschule HannoverChemisches InstitutHannoverGermany
  3. 3.EMBL c/o DESYHamburgGermany

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