The fermentative metabolism of Rhodospirillum rubrum (strain Ha, F1, S1) was studied after transfering the cells from aerobic to anaerobic dark culture conditions. Pyruvate was metabolized mainly to acetate and formate, and to a lesser extent to CO2 and priopionate, by all strains. Therefore, pyruvate formate lyase would appear to be the characteristic key enzyme of the dark anaerobic fermentation metabolism in R. rubrum. Strain F1 and S1 metabolized the formate further to H2 and CO2. It is concluded that this cleavage was catalysed by a formate hydrogen lyase system. Strain Ha was unable to metabolize formate. The cleavage of formate and the synthesis of poly-beta-hydroxy-butyric acid were increased by a low pH value (approximately 6.5). Fermentation equations and schemes of the pyruvate metabolism are discussed.
Pyruvate fermentation in Rhodospirillum rubrum (strains F1, S1, and Ha) was investigated using cells precultured on different substrates anaerobically in the light and than transferred to anaerobic dark conditions. Pyruvate formate lyase was always the key enzyme in pyruvate fermentation but its activity was lower than in cells which have been precultured aerobically in darkness. The preculture substrate also had a clear influence on the pyruvate formate lyase activity. Strains F1 and S1 metabolized the produced formate further to H2 and CO2. A slight production of CO2 from pyruvate, without additional H2-production, could also be detected. It was concluded from this that under anaerobic dark conditions a pyruvate dehydrogenase was also functioning. On inhibition of pyruvate formate lyase the main part of pyruvate breakdown was taken over by pyruvate dehydrogenase. When enzyme synthesis was inhibited by chloramphenicol, propionate production in contrast to formate production was not affected. Protein synthesis was not significant during anaerobic dark culture. Bacteriochlorophyll, however, showed, after a lag phase, a clear rise.
Experiments with 14C labelled propionyl-CoA, methylmalonyl-CoA and succinyl-CoA showed that these compounds are intermediates of propionate synthesis in fermentative metabolism of Rhodospirillum rubrum. The rate of propionate and succinate production is dependent on the CO2 concentration of the medium. There is, however, no evidence for a transcarboxylation, and high concentrations of propionate in the medium did not inhibit propionate synthesis as in the case in propionibacteria. PEP-carboxykinase (EC 4.1.1.32) and propionyl-CoA-carboxylase (EC 6.4.1.3) showed high activities, whereas the other two PEP-carboxylases (EC 4.1.1.31, EC 4.1.1.38), and the pyruvate-carboxylase (EC 4.1.1.1.) showed only very low activity. It is probable that in pyruvate fermentation metabolism of R. rubrum no specific enzymes are activated for propionate formation and all enzymes are still present from aerobic or phototrophic preculture.
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