Structure of a bacterial photosynthetic membrane: integrity of reaction centers following proteolysis and detergent solubilization.
The photosynthetic membranes of the purple bacterium Rhodopseudomonas viridis are composed of a semi-crystalline lattice of subunits. Proteolysis of isolated membranes with trypsin or pronase results in the degradation of polypeptides associated with the photosynthetic reaction center. However, two low molecular weight peptides which may form the light-harvesting complex survive the enzymatic treatment. The proteolysis does not affect the major absorbance peak (830 nm) associated with the reaction center. However, treatment of proteolyzed membranes with detergents such as LDAO abolishes the 830 nm absorbance peak. The 830 nm peak is stable following LDAO solubilization of non-proteolyzed membranes. These results suggest that a combination of covalent and non-covalent interactions are important in maintaining the configuration of the reaction center, and are consistent with a model of membrane organization in which the light-harvesting components are buried in a lipid phase of the membrane and reaction center components form the large structures which electron microscope studies have shown to extend from either membrane surface.
D001426:Bacterial Proteins / Q000302:isolation & purification*; D003902:Detergents; D004123:Dimethylamines; D045322:Photosynthetic Reaction Center Complex Proteins; D011402:Pronase; D012241:Rhodopseudomonas / Q000032:analysis*; D012995:Solubility; D013053:Spectrophotometry; D013055:Spectrophotometry, Infrared; D013501:Surface-Active Agents; D014357:Trypsin
D001426:Bacterial Proteins; D003902:Detergents; D004123:Dimethylamines; D045322:Photosynthetic Reaction Center Complex Proteins; D013501:Surface-Active Agents; C014518:dodecyldimethylamine oxide; D014357:Trypsin; D011402:Pronase