Freeze-fracture analysis of thylakoid membranes and photosystem I and II enriched fractions from Phormidium laminosum.
Thylakoid membranes of the thermophilic cyanobacterium Phormidium laminosum have been fractionated into photosystem II and photosystem I particles. These fractions have been characterized by their partial electron transport activities, and biochemical and spectral properties. Exoplasmic fracture face and protoplasmic fracture face particles in the unfractionated thylakoid membranes were shown to correspond in size to particles in freeze-fractured photosystem II and photosystem I fractions, respectively. Differences between the histograms of the thylakoid membrane protoplasmic fracture face particles and the isolated photosystem I particles suggest that in addition to photosystem I complexes some of the particles on the thylakoid protoplasmic fracture face may be related to cytochrome b/f complexes, the hydrophobic component of the coupling factor, or respiratory complexes.
D002462:Cell Membrane / Q000032:analysis / Q000648:ultrastructure*; D002734:Chlorophyll / Q000032:analysis; D000458:Cyanobacteria / Q000648:ultrastructure*; D005614:Freeze Fracturing; D045342:Light-Harvesting Protein Complexes; D008854:Microscopy, Electron; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D045332:Photosystem II Protein Complex; D010940:Plant Proteins / Q000032:analysis; D013054:Spectrophotometry, Atomic
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D002734:Chlorophyll