Correlation between the ATP synthetic active state and the ATP hydrolytic active state in chloroplast ATP synthase-ATPase complex CF0 . CF1.
Illumination of chloroplast thylakoids activates ATP synthase-ATPase complex CF0 . CF1. The time course of ATP synthesis is linear if ADP and Pi are added before or simultaneously with illumination. ATP synthesis initiated by adding the substrates in the light exhibits a curvilinear time course with a low initial rate (Vi). Vi, but not the rate at a steady state, decreases with increasing preillumination time with a half-time of 2 s. Coincident with this decrease in Vi, activation of ATP hydrolysis takes place. In the postillumination dark, restoration of Vi is observed: Vi increases with increasing time intervals between the end of illumination and the addition of the substrates with simultaneous reillumination (half-time of 3 s). Coincident with this restoration of Vi, inactivation of ATP hydrolysis takes place. Such an increase in Vi in the postillumination dark is not observed in thylakoids pretreated with N-ethylmaleimide. These results suggest the following: in the light, the ATP synthetically active, but ATP hydrolytically inactive state (Es) converts to the ATP hydrolytically active, but ATP synthetically inactive (or less active) state (Eh) in the absence of ADP and Pi. The N-ethylmaleimide pretreatment inhibits this process. In the postillumination dark, the reverse conversion takes place.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology*; D003624:Darkness; D005033:Ethylmaleimide / Q000494:pharmacology; D007700:Kinetics; D008027:Light; D010944:Plants / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D005033:Ethylmaleimide