ATP hydrolysis caused by acid-base transition of spinach chloroplasts

1967 ◽  
Vol 120 (2) ◽  
pp. 365-370 ◽  
Author(s):  
Joel H. Kaplan ◽  
Ernest Uribe ◽  
A.T. Jagendorf
1987 ◽  
Vol 42 (3) ◽  
pp. 231-236 ◽  
Author(s):  
Günter Schmidt ◽  
Peter Gräber

The conditions for optimal rates of ATP hydrolysis catalyzed by the chloroplast ATP-synthase (ATPase), CF0F1, after isolation and reconstitution into asolectin liposomes have been investi­gated. The rate of ATP hydrolysis was measured either after oxidation of CF0F1 (by incubation with iodosobenzoate) or after reduction of CFoF, (by incubation with dithiothreitol). In both cases a rate of about 1-2 ATP (CF0F1·s)-1 was observed under uncoupled conditions. If the proteoliposomes are first energized by an acid-base transition and a K+ /valinomycin diffusion poten­tial, the uncoupled rate of ATP hydrolysis is about 1-2 ATP (CF0F1 ·s) 1 for the oxidized enzyme and about 20 for the reduced species. This rate is about a factor 2 smaller than that observed in chloroplasts under the same conditions


1974 ◽  
Vol 76 (1) ◽  
pp. 233-235 ◽  
Author(s):  
Tatsuo OKU ◽  
Kazuo HOSOI ◽  
Gilbu SOE ◽  
Tomisaburo KAKUNO ◽  
Takekazu HORIO

1967 ◽  
Vol 22 (10) ◽  
pp. 1051-1054 ◽  
Author(s):  
Reinhard Bachofen ◽  
Ingrid Specht-Jürgensen

Chloroplasts possess an ATP-Pa-exchange activity, which is induced by a transition from acid to base. The reaction is dependant on the presence of Mg2⨁ and a reducing agent, DTT. The exchange reaction induced by acid-base transition has properties similar to the light-triggered ATP–Pa-exchange and the ATP-synthesis induced by acid-base transition.


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