The assembly of protein subunits and cofactors in photosystem I.
The recently determined crystal structures of photosystems I and II at 2.5 A and 3.8 A resolution, respectively, have improved the structural basis for understanding the processes of light trapping, exciton transfer and electron transfer occurring in the primary steps of oxygenic photosynthesis. Understanding the assembly of the 12 protein subunits and 128 cofactors in photosystem I allows us to study the possible functions of the individual players in this protein-cofactor complex.
Saenger
Wolfram
W
Institut für Chemie/Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195, Berlin, Germany. saenger@chemie.fu-berlin.de
Jordan
Patrick
P
Krauss
Norbert
N
D002338:Carotenoids / Q000737:chemistry / Q000378:metabolism; D002734:Chlorophyll / Q000737:chemistry / Q000378:metabolism; D000077194:Chlorophyll A; D000458:Cyanobacteria / Q000737:chemistry / Q000502:physiology; D004579:Electron Transport; D045342:Light-Harvesting Protein Complexes; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry; D008958:Models, Molecular; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D045331:Photosystem I Protein Complex; D011487:Protein Conformation; D021122:Protein Subunits
D045342:Light-Harvesting Protein Complexes; D008055:Lipids; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D021122:Protein Subunits; D002734:Chlorophyll; D002338:Carotenoids; D000077194:Chlorophyll A