On the coordination and oxidation states of the active-site copper ion in prokaryotic Cu,Zn superoxide dismutases

M. E. Stroppolo, S. Nuzzo, A. Pesce, C. Rosano, A. Battistoni, M. Bolognesi, S. Mobilio, A. Desideri

Research output: Contribution to journalArticlepeer-review

Abstract

The active-site copper ion of the prokaryotic Cu,Zn superoxide dismutase from P. leiognathi is found to undergo reversible reduction upon irradiation of the protein solution with a high-intensity X-ray beam from a third-generation synchrotron source. The same phenomenon is observed for the enzyme crystals, whose diffraction pattern has been obtained from synchrotron sources. In this case the active-site copper-ligand coordination bond lengths and in particular the Cu-NE2(His61) distance are consistent with a copper ion in the reduced state. These results are in line with previous studies on the eukaryotic Cu,Zn superoxide dismutases and suggest the conservation of an identical catalytic mechanism in both the prokaryotic and eukaryotic enzymes.

Original languageEnglish
Pages (from-to)579-582
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume249
Issue number3
DOIs
Publication statusPublished - Aug 28 1998

Keywords

  • Bacterial Cu, Zn superoxide dismutase
  • Copper coordination redox state
  • X-ray diffraction
  • XANES

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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