A structural investigation of cytochrome c binding to photosynthetic reaction centers in reconstituted membranes.
Mammalian cytochrome c can effectively replace bacterial cytochrome c2 as the electron donor to the bacterial photosynthetic reaction center in either the natural chromatophore or a reconstituted reaction center/phospholipid membrane. In this paper, the reconstituted membrane was used to describe the nature of cytochrome c binding to the reaction center, the location of bound cytochrome c in the membrane profile and the perturbation of the reaction center and phospholipid profile structures indicated by cytochrome c binding. These structural studies utilized the combined techniques of X-ray and neutron diffraction.
D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D006736:Horses; D007700:Kinetics; D009206:Myocardium / Q000378:metabolism; D009502:Neutrons; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding; D013057:Spectrum Analysis; D014961:X-Ray Diffraction
D003574:Cytochrome c Group; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins