A preparation of chromatophores from Rhodopseudomonas capsulata is described in which NADH oxidase activity is stimulated by uncouplers and during ATP synthesis, and is strongly inhibited upon illumination. The inhibition is completely reversed by addition of a protonophore or the combination of valinomycin, nigericin and K + , thus demonstrating that the proton electro-chemical gradient generated by light-driven cyclic electron flow is responsible for the inhibition of respiration. By analogy it is suggested that light-induced inhibition of respiration in intact cells of photosynthetic bacteria is also controlled by the proton electrochemical gradient. The results show that all chromatophores that possess oxidase activity must also have light-driven cyclic electron flow pathways. This has implications for experiments in which carotenoid band shifts and distributions of permeant anions have been compared as indicators of membrane potentials in chromatophores.