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Conditions for washed, spinach thylakoid membranes to catalyze cyclic phosphorylation using ferredoxin as the cofactor for electron transfer have been re-examined. It was found necessary to “redox poise” the system; however, the best method to accomplish the poising seemed to be the use of a reductant (glucose-6-phosphate) and not by optimizing the rate of phosphorylation with 3- (3,4-dichlorophenyl)-1,1-dimethyl urea (DCMU). Under these conditions, ferredoxin catalyzed cyclic phosphorylation was found to be sensitive to the inhibitors antimycin A and dibromothymo- quinone (DBMIB). The inhibition of ferredoxin catalyzed cyclic phosphorylation by DBMIB, but not by antimycin A, was completely reversed by N, N, N′ N′-tetramethyl-p-phcnylenediamine (TMPD). These data are taken as further support for the function of plastoquinone in ferredoxin catalyzed cyclic phosphorylation. The effect of TMPD in reversing the DBMIB inhibition is inter­preted as the formation of a TMPD bypass on the internal side of the thylakoid membrane around the DBMIB site of inhibition.

Ferredoxin Catalyzed Cyclic Photophosphorylation: Reversal of Dibromothymoquinone Inhibition by N ,N ,N′,N′-Tetramethyl-p-phenylenediamine