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. 1971 Oct;108(1):334–342. doi: 10.1128/jb.108.1.334-342.1971

Heterotrophic Metabolism of the Chemolithotroph Thiobacillus ferrooxidans

Robert Tabita 1, D G Lundgren 1
PMCID: PMC247071  PMID: 4399339

Abstract

Glucose-6-phosphate dehydrogenase and the enzymes of the Entner-Doudoroff pathway, 6-phosphogluconate dehydrase and 2-keto-3-deoxy-6-phosphogluconate aldolase (assayed together), are induced during heterotrophic growth of Thiobacillus ferrooxidans on an iron-glucose-supplemented medium or on glucose alone. By contrast, autotrophic cells (iron-grown) contain low levels of these enzymes. Fructose 1, 6-diphosphate aldolase, an enzyme of the Embden-Meyerhof pathway, is present at low levels irrespective of the growth medium, suggesting that this enzyme is not involved in energy-yielding reactions but merely provides intermediates for biosynthesis. The Entner-Doudoroff and pentose-phosphate pathways are the principle means through which glucose is dissimilated and is presumed to be concerned with energy production. Isotopic studies showed that a high rate of CO2 formation from specifically labeled glucose came from carbon atoms 1 and 4. An unexpectedly high rate of evolution of CO2 also came from carbon 6, suggesting that the triose phosphate formed during glucose breakdown and specifically as a result of 2-keto-3-deoxy-6-phosphogluconate aldolase activity, was metabolized via some unorthodox metabolic route. Cells grown in the iron-supplemented and glucose-salts media have a complete tricarboxylic acid cycle, whereas autotrophically grown T. ferrooxidans lacked both α-ketoglutarate dehydrogenase and reduced nicotinamide adenine dinucleotide oxidase. Two isocitrate dehydrogenases [nicotinamide adenine dinucleotide (NAD) and NAD phosphate (NADP) specific] were present. NAD-linked enzyme was constitutive, whereas the NADP-linked enzyme was induced upon adaptation of autotrophic cells to heterotrophic growth.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ARRIGONI O., SINGER T. P. Limitations of the phenazine methosulphate assay for succinic and related dehydrogenases. Nature. 1962 Mar 31;193:1256–1258. doi: 10.1038/1931256a0. [DOI] [PubMed] [Google Scholar]
  2. Andersen K. J., Lundgren D. G. Enzymatic studies of the iron-oxidizing bacterium, Ferrobacillus ferrooxidans: evidence for a glycolytic pathway and Krebs cycle. Can J Microbiol. 1969 Jan;15(1):73–79. doi: 10.1139/m69-012. [DOI] [PubMed] [Google Scholar]
  3. Butler R. G., Umbreit W. W. Reduced nicotinamide adenine dinucleotide oxidase and alpha-ketoglutaric dehydrogenase activity by Thiobacillus thiooxidans. J Bacteriol. 1969 Feb;97(2):966–967. doi: 10.1128/jb.97.2.966-967.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Eisenberg R. C., Dobrogosz W. J. Gluconate metabolism in Escherichia coli. J Bacteriol. 1967 Mar;93(3):941–949. doi: 10.1128/jb.93.3.941-949.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GOTTSCHALK G., EBERHARDT U., SCHLEGEL H. G. VERWERTUNG VON FRUCTOSE DURCH HYDROGENOMONAS H 16. (I.) Arch Mikrobiol. 1964 Apr 2;48:95–108. [PubMed] [Google Scholar]
  6. KITOS P. A., WANG C. H., MOHLER B. A., KING T. E., CHELDELIN V. H. Glucose and gluconate dissimilation in Acetobacter suboxydans. J Biol Chem. 1958 Dec;233(6):1295–1298. [PubMed] [Google Scholar]
  7. Keele B. B., Jr, Hamilton P. B., Elkan G. H. Glucose catabolism in Rhizobium japonicum. J Bacteriol. 1969 Mar;97(3):1184–1191. doi: 10.1128/jb.97.3.1184-1191.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kuehn G. D., McFadden B. A. Enzymes of the Entner-Doudoroff path in fructose-grown Hydrogenomonas eutropha. Can J Microbiol. 1968 Nov;14(11):1259–1260. doi: 10.1139/m68-209. [DOI] [PubMed] [Google Scholar]
  9. Matin A., Rittenberg S. C. Regulation of glucose metabolism in Thiobacillus intermedius. J Bacteriol. 1970 Oct;104(1):239–246. doi: 10.1128/jb.104.1.239-246.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Peck H. D., Jr Energy-coupling mechanisms in chemolithotrophic bacteria. Annu Rev Microbiol. 1968;22:489–518. doi: 10.1146/annurev.mi.22.100168.002421. [DOI] [PubMed] [Google Scholar]
  11. Perry J. J., Evans J. B. Glucose catabolism in Micrococcus sodonensis. J Bacteriol. 1967 Jun;93(6):1839–1846. doi: 10.1128/jb.93.6.1839-1846.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. RACKER E. Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids. Biochim Biophys Acta. 1950 Jan;4(1-3):211–214. doi: 10.1016/0006-3002(50)90026-6. [DOI] [PubMed] [Google Scholar]
  13. SMITH R. A., GUNSALUS I. C. Isocitritase; enzyme properties and reaction equilibrium. J Biol Chem. 1957 Nov;229(1):305–319. [PubMed] [Google Scholar]
  14. Shafia F., Wilkinson R. F., Jr Growth of Ferrobacillus ferrooxidans on organic matter. J Bacteriol. 1969 Jan;97(1):256–260. doi: 10.1128/jb.97.1.256-260.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Silver M., Lundgren D. G. Sulfur-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans). Can J Biochem. 1968 May;46(5):457–461. doi: 10.1139/o68-069. [DOI] [PubMed] [Google Scholar]
  16. Silver M., Margalith P., Lundgren D. G. Effect of glucose on carbon dioxide assimilation and substrate oxidation by Ferrobacillus ferrooxidans. J Bacteriol. 1967 Jun;93(6):1765–1769. doi: 10.1128/jb.93.6.1765-1769.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Smith A. J., Hoare D. S. Acetate assimilation by Nitrobacter agilis in relation to its "obligate autotrophy". J Bacteriol. 1968 Mar;95(3):844–855. doi: 10.1128/jb.95.3.844-855.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Smith A. J., London J., Stanier R. Y. Biochemical basis of obligate autotrophy in blue-green algae and thiobacilli. J Bacteriol. 1967 Oct;94(4):972–983. doi: 10.1128/jb.94.4.972-983.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tabita R., Lundgren D. G. Glucose-6-phosphate dehydrogenase from the chemolithotroph Thiobacillus ferrooxidans. J Bacteriol. 1971 Oct;108(1):343–352. doi: 10.1128/jb.108.1.343-352.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Tabita R., Lundgren D. G. Utilization of glucose and the effect of organic compounds on the chemolithotroph Thiobacillus ferrooxidans. J Bacteriol. 1971 Oct;108(1):328–333. doi: 10.1128/jb.108.1.328-333.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Trudinger P. A., Kelly D. P. Reduced nicotinamide adenine dinucleotide oxidation by Thiobacillus neapolitanus and Thiobacillus strain C. J Bacteriol. 1968 May;95(5):1962–1963. doi: 10.1128/jb.95.5.1962-1963.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. WANG C. H., STERN I., GILMOUR C. M., KLUNGSOYR S., REED D. J., BIALY J. J., CHRISTENSEN B. E., CHELDELIN V. H. Comparative study of glucose catabolism by the radiorespirometric method. J Bacteriol. 1958 Aug;76(2):207–216. doi: 10.1128/jb.76.2.207-216.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wang W. S., Lundgren D. G. Poly-beta-hydroxybutyrate in the chemolithotrophic bacterium Ferrobacillus ferrooxidans. J Bacteriol. 1969 Feb;97(2):947–950. doi: 10.1128/jb.97.2.947-950.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Watson B. F., Dworkin M. Comparative intermediary metabolism of vegetative cells and microcysts of Myxococcus xanthus. J Bacteriol. 1968 Nov;96(5):1465–1473. doi: 10.1128/jb.96.5.1465-1473.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]

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