Oligomycin-insensitive incorporation of ^<32>P into chloroplast protein by illumination

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^<32>P incorporation into the protein fraction of chloroplast fragments by short illumination was investigated under various phosphorylating conditions. ^<32>P incorporation was generally accompanied by cyclic and non-cyclic photophosphorylations and also by formation of a high energy intermediate "X_E " However, the addition of a DPIP-ascorbate couple caused inhibition of ^<32>P incorporation, while ATP formation proceeded. Effects of inhibitors and uncouplers of photophosphorylation on the formation of protein-bound ^<32>P were generally similar to those on ATP formation. AT^<32>P was not utilized for protein-bound ^<32>P formation in the dark by chloroplast fragments, but its radioactivity was transferred into the chloroplast protein fraction in the light. Oligomycin inhibited ATP formation but did not inhibit protein-bound ^<32>P formation. m-Cl-CCP blocked both reactions. This suggests that protein-bound ^<32>P is not an actual intermediate in the phosphorylative process leading to formation of ATP. It is probably formed on a side pathway from an intermediate of ATP formation. Analyses of protein-bound ^<32>P after digestion with protease and lipase showed that the ^<32>P incorporated was bound to peptides in chloroplast lamellae. The possible form of this bound ^<32>P is discussed.
日本植物生理学会の論文