Abstract
Chromatophores isolated from Rhodospirillum rubrum contain in addition to their photophosphorylation mechanism a number of the energy-linked functions found in rat liver and ox-heart submitochondrial particles. Like submitochondrial particles, the chromatophores catalyze an electron transport coupled phosphorylation of ADP to ATP [l] , energylinked ion transport [2], the energy dependent reduction of NAD+ by succinate [3] , and an energy-linked transhydrogenation between NADH and NADP+ [4]. In addition, chromatophores are able to couple the synthesis of pyrophosphate to electron transport [S]. Chromatophores further resemble submitochondrial particles in that they contain ATPase activity. The ATPase activity has been postulated to be a result of a reversal of the phosphorylation mechanism and the hydrolytic cleavage of an energized intermediate [6]. Studies of the coupling factor, F,, from ox-heart mitochondria suggested that mitochondrial ATPase represents the terminal enzyme of the phosphorylation mechanism [7]. In analogy with the mitochondrial and chromatophore ATPase activity, the inorganic pyrophosphatase activity of R. rubrum has been pos-
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