These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: On the coordination and oxidation states of the active-site copper ion in prokaryotic Cu,Zn superoxide dismutases.
    Author: Stroppolo ME, Nuzzo S, Pesce A, Rosano C, Battistoni A, Bolognesi M, Mobilio S, Desideri A.
    Journal: Biochem Biophys Res Commun; 1998 Aug 28; 249(3):579-82. PubMed ID: 9731178.
    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.
    [Abstract] [Full Text] [Related] [New Search]