Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Buchkapitel

New Insights into the X-Ray Structure of the Reaction Center from Rhodopseudomonas viridis

MPG-Autoren
/persons/resource/persons137768

Lancaster,  C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137800

Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Lancaster, C. R. D., & Michel, H. (1996). New Insights into the X-Ray Structure of the Reaction Center from Rhodopseudomonas viridis. In M.-E. Michel-Beyerle (Ed.), The Reaction Center of Photosynthetic Bacteria (pp. 23-35). Berlin, Heidelberg: Springer.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-649E-7
Zusammenfassung
Light-induced electron transfer in the reaction center (RC) is coupled to the uptake of protons from the cytoplasm at the binding site of the secondary quinone (QB). With quinone reconstitution, a higher QB occupancy has been obtained in the Rhodopseudomonas (Rp.) viridis RC crystals, which, after X-ray analysis, has resulted in a well-defined QB-site model. On the basis of this new model and the structure of a stigmatellin-RC complex, a new understanding of QB binding, particularly concerning the role of Ser L223, has emerged. Furthermore, with high quality data collected on RC complexes with atrazine and two chiral atrazine derivatives, it has been possible to describe the exact nature of triazine binding and its effect on the structure of the protein. The new data are of sufficient quality to improve the original model also in other parts, e.g. regarding the asymmetry of binding of the primary quinone (QA), the structure of the carotenoid, and additional tightly-bound water molecules.