Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 327546
Title Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation
Author(s) Aragao, D.; Macedo, S.; Mitchell, E.P.; Romao, C.V.; Liu, M.Y.; Frazao, C.; Saraiva, L.M.; Xavier, A.V.; LeGall, J.; Dongen, W.M.A.M. van; Hagen, W.R.; Teixeira, M.; Carrondo, M.A.; Lindley, P.
Source Journal of Biological Inorganic Chemistry 8 (2003). - ISSN 0949-8257 - p. 540 - 548.
Department(s) Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2003
Keyword(s) electron-density maps - escherichia-coli - angstrom resolution - nitrite reductase - sulfite reductase - prismane protein - identification - spectroscopy - refinement - errors
Abstract The hybrid cluster proteins from the sulfate reducing bacteria Desulfovibrio desulfuricans ATCC 27774 (Dd) and Desulfovibrio vulgaris strain Hildenborough(Dv) have been isolated and crystallized anaerobically. In each case, the protein has been reduced with dithionite and the crystal structure of the reduced form elucidated using X-ray synchrotron radiation techniques at 1.25 Angstrom and 1.55 Angstrom resolution for Dd and Dv, respectively. Although the overall structures of the proteins are unchanged upon reduction, there are significant changes at the hybrid cluster centres. These include significant movements in the position of the iron atom linked to the persulfide moiety in the oxidized as-isolated proteins and the sulfur atom of the persulfide itself. The nature of these changes is described and the implications with respect to the function of hybrid cluster proteins are discussed.
There are no comments yet. You can post the first one!
Post a comment
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.