Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark.
The structure of the Blastochloris viridis photosynthetic reaction center has been determined at 100 K by flash-freezing crystals. A data set to 2.2 A resolution provides a well determined model of the wild-type protein. Of particular interest are the position, occupancy and heterogeneity of the Q(B)-binding site. Data were also collected from a crystal frozen immediately after illumination. The data support predominant binding of Q(B) in the proximal position in both the neutral and charge-separated states.
Baxter
Richard H G
RH
Department of Chemistry, University of Chicago, 5735 South Ellis Avenue, Chicago, IL 60637, USA.
Seagle
Brandon Luke
BL
Ponomarenko
Nina
N
Norris
James R
JR
D001665:Binding Sites; D003451:Cryoprotective Agents / Q000737:chemistry; D003460:Crystallization; D003624:Darkness; D005615:Freezing; D006540:Herbicides / Q000494:pharmacology; D008027:Light; D008958:Models, Molecular; D010788:Photosynthesis / Q000502:physiology*; D020560:Proteobacteria / Q000378:metabolism*; D011809:Quinones / Q000737:chemistry; D014451:Ubiquinone / Q000378:metabolism; D014867:Water / Q000737:chemistry
D003451:Cryoprotective Agents; D006540:Herbicides; D011809:Quinones; D014867:Water; D014451:Ubiquinone; C030571:ubiquinone 9