Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation.
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 A and 1.55 A 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.
Aragão
David
D
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.|European Synchrotron Radiation Facility, BP 220, 38043 Cedex, Grenoble , France.
Macedo
Sofia
S
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.|European Synchrotron Radiation Facility, BP 220, 38043 Cedex, Grenoble , France.
Mitchell
Edward P
EP
European Synchrotron Radiation Facility, BP 220, 38043 Cedex, Grenoble , France.
Romão
Célia V
CV
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.
Liu
Ming Y
MY
Department of Biochemistry, University of Georgia, Athens, GA , 30602, USA.
Frazão
Carlos
C
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.
Saraiva
Lígia M
LM
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.
Xavier
António V
AV
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.
LeGall
Jean
J
Department of Biochemistry, University of Georgia, Athens, GA , 30602, USA.
van Dongen
Walter M A M
WMAM
Department of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA , Wageningen, The Netherlands.
Hagen
Wilfred R
WR
Kluyver Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC , Delft, The Netherlands.
Teixeira
Miguel
M
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.
Carrondo
Maria A
MA
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal.
Lindley
Peter
P
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, Apartado 127, 2781-901 , Oeiras, Portugal. lindley@itqb.unl.pt.|European Synchrotron Radiation Facility, BP 220, 38043 Cedex, Grenoble , France. lindley@itqb.unl.pt.
D003460:Crystallization; D018360:Crystallography, X-Ray; D003901:Desulfovibrio / Q000737:chemistry* / Q000528:radiation effects; D016969:Desulfovibrio vulgaris / Q000737:chemistry* / Q000528:radiation effects; D015151:Immunoblotting; D008958:Models, Molecular; D008968:Molecular Conformation; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry* / Q000528:radiation effects; D017356:Synchrotrons
D011506:Proteins; D010088:Oxidoreductases; C021402:hydroxylamine reductase