Reconstitution of photosynthetic energy conservation. II. Photophosphorylation in liposomes containing photosystem-I reaction center and chloroplast coupling-factor complex.
Photophosphorylation has been reconstituted in a liposomal system containing reaction centers of photosystem I and coupling-factor complex, both highly purified from spinach chloroplasts. This energy-converting model system was put together by diluting the preparation of the coupling-factor complex with an aqueous suspension of proteolipid vesicles, preformed from photosystem-I reaction centers and soybean phospholipids by sonication. In the presence of reduced N-methyl-phenazonium methosulfate the system catalyzed photophosphorylation with rates up to 50 mumol ATP formed x mg chlorophyll-1 x h-1, which was sensitive to uncouplers and to N,N'-dicyclohexyl-carbodiimide. The properties of the system in comparison to chloroplasts is discussed.
D000643:Ammonium Chloride / Q000494:pharmacology; D002734:Chlorophyll / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D004579:Electron Transport / Q000187:drug effects; D007700:Kinetics; D008081:Liposomes; D008773:Methylphenazonium Methosulfate / Q000494:pharmacology; D008954:Models, Biological; D010785:Photophosphorylation / Q000187:drug effects; D010788:Photosynthesis; D010944:Plants / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D014634:Valinomycin / Q000494:pharmacology
D008081:Liposomes; D000643:Ammonium Chloride; D002734:Chlorophyll; D014634:Valinomycin; D008773:Methylphenazonium Methosulfate; D006180:Proton-Translocating ATPases