The chromatophore of Rhodospirillum rubrum was shown to possess enzymes for the activation and reduction of inorganic sulfate. The chromatophore was able to synthesize 3'-phosphoadenosine 5'-phosphosulfate (PAPS), using either exogenous adenosine triphosphate (ATP) or ATP synthesized via photophosphorylation. Light was required for the reduction of sulfate to a volatile form, presumably sulfite. Light enhanced the incorporation of sulfate-sulfur into cystine, cysteine, and cysteic acid of the chromatophore. This incorporation was probably the result of exchange reactions of reduced sulfur, not the result of net synthesis. The 100:1 ratio of the activation to reduction of sulfate and the inhibition of the reduction by exogenous ATP suggested that PAPS might not be the substrate for chromatophoral sulfate reduction. The bacterial chromatophore has been shown to mediate not only a number of photochemical reactions but also several dark reactions (Frenkel, 1959b). Two of the more physiologically significant photochemical reactions are the lightinduced esterification of phosphate (Frenkel, 1956) and the light-induced reduction of pyridine nucleotide (Frenkel, 1959a). Rhodospirillum rubrum is able to satisfy its sulfur requirement by assimilating inorganic sulfate either in the light or dark. As R. rubrum has been shown to reduce sulfate photochemically (Ibanez and Lindstrom, 1959), we wished to determine the relationship between the chromatophoral photometabolism