Photoreduction of the artificial electron acceptor, cytochrome c, by isolated spinach chloroplasts in the absence of added catalyst has been found to be resistant to inhibition by 10 mᴍ salicyl aldoxime. This contrasts with the pronounced inhibition of the photoreduction of both 2,6-dichloro-phenolindophenol and ferricyanide over a range of electron flow rates, and indicates an inhibition on the acceptor side rather than on the donor side of photosystem 2 (PS2). All photoreductions were susceptible to inhibition by 3-(3′,4′-dichlorophenyl)-1, 1-dimethyl urea (DCMU). Salicyl aldoxime (1 -10 mᴍ) inhibited electron flow from PS2 to P700, and also altered the chlorophyll fluorescence induction of dark-adapted chloroplasts. Salicylaldoxime concentrations up to 5 mM did not change the initial fluorescence level, F 0 , or the initial slope, (dF/dt) 0 , but lowered the final steady state fluorescence level, F m , and the value of p 0 [p 0 = (F m - F 0 )/F m ] ; an effect similar to that seen on 1 mᴍ ferricyanide addition, thus indicating an induced oxidation of the fluorescence quencher, Q. Both DCMU and orthophenanthroline, which block electron transport directly after Q, caused an increase in (dF/dt) 0 , F 0 and F m but left p 0 unchanged. This contrasted with the effect of salicylaldoxime. It is proposed that salicylaldoxime inhibits electron transport from PS2 to photosystem 1, at a site which can probably be identified with the plastoquinone pool, by inducing a cyclic flow of electrons around PS2. Cytochrome c, under the conditions used, appears to be photoreduced at a site close to the secondary electron acceptor, R, of PS2.