The activation and inactivation of the Dunaliella salina chloroplast coupling factor 1 (CF1) in vivo and in situ.
Preillumination of intact cells of the eukaryotic, halotolerant, cell-wall-less green alga Dunaliella salina induces a dark ATPase activity the magnitude of which is about 3-5-fold higher than the ATPase activity observed in dark-adapted cells. The light-induced activity arises from the activation and stabilization in vivo of chloroplast coupling factor 1 (CF1). This activity, approximately 150-300 mumol ATP hydrolyzed/mg Chl per h, rapidly decays (with a half-time of about 6 min at room temperature) in intact cells but only slowly decays (with a half-time of about 45 min at room temperature) if the cells are lysed by osmotic shock immediately after illumination. The activated form of the ATPase in lysed cells is inhibited if the membranes are treated with ferri- but not ferrocyanide, suggesting that the stabilization of the activated form of CF1 is due to the reduction of the enzyme in vivo in the light.
D000460:Chlorophyta / Q000201:enzymology; D002736:Chloroplasts / Q000201:enzymology*; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects / Q000528:radiation effects; D005292:Ferricyanides / Q000494:pharmacology; D008027:Light; D009997:Osmotic Pressure; D010084:Oxidation-Reduction; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D005292:Ferricyanides; C007931:hexacyanoferrate III; D006180:Proton-Translocating ATPases; D004229:Dithiothreitol