Archives of Microbiology

, Volume 144, Issue 1, pp 78–83 | Cite as

ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans

  • Jens Paulsen
  • Achim Kröger
  • Rudolf K. Thauer
Original Papers


The oxidation of succinate with elemental sulphur in Desulfuromonas acetoxidans was investigated using a membrane preparation of this bacterium. The following results were obtained:
  1. 1.

    The preparation catalyzed the oxidation of succinate with sulphur and NAD. These reactions were dependent on ATP and were abolished by the presence of protonophores or dicyclohexylcarbodiimide (DCCD).

  2. 2.

    The membrane preparation also catalyzed the reduction of fumarate with H2S or with NADH. These activities were not dependent on ATP and were not affected by protonophores or DCCD.

  3. 3.

    By extraction-reincorporation experiments it could be shown that menaquinone is involved in electron transport between H2S and fumarate and between NADH and fumarate.

  4. 4.

    The membrane fraction catalyzed the reduction of the water-soluble menaquinone-analogue dimethylnaphthoquinone (DMN) by succinate, H2S, or NADH, and the oxidation of DMNH2 by fumarate. These activities were not dependent on the presence of menaquinone and were not influenced by ATP.

  5. 5.

    The activities involving succinate oxidation or fumarate reduction were similarly sensitive to 2(n-nonyl)-4-hydroxyquinoline-N-oxide, while H2S and NADH oxidation by DMN were not affected by the inhibitor.


It is concluded that the catabolism of D. acetoxidans involves the energy-driven oxidation of succinate with elemental sulphur or NAD as electron acceptors and that menaquinone is a component of the electron transport chain catalyzing these reactions.

Key words

Desulfuromonas acetoxidans Succinate oxidation Sulphur reduction Acetate oxidation Citric acid cycle Reverse of electron transport Menaquinone ATP synthase Succinate dehydrogenase Sulphur reductase NADH dehydrogenase 

Non-standard abbreviations












Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Anderson BM, Kaplan NO (1959) Enzymatic studies with analogues of diphosphopyridine nucleotide. J Biol Chem 234:1226–1232Google Scholar
  2. Bache R, Kroneck PMH, Merkle H, Beinert H (1983) A survey of EPR-detectable components in sulfur-reducing bacteria. Biochim Biophys Acta 722:417–426Google Scholar
  3. Bode CH, Goebell H, Stähler E (1968) Zur Eliminierung von Trübungsfehlern bei der Eiweißbestimmung mit der Biuretmethode. Z Klin Chem Klin Biochem 5:419–422Google Scholar
  4. Büchel KH, Korte F (1965) Hemmung photosynthetischer Reaktionen durch NH-acide Imidazole and Benzimidazole. Angew Chem 20:911–912Google Scholar
  5. Erecinska M, Wilson DF (1981) Inhibitors of mitochondrial functions. Pergamon Press, Oxford New York Toronto Sydney Paris FrankfurtGoogle Scholar
  6. Futai M, Kanazawa H (1983) Structure and function of protontranslocating adenosine triphosphatase (F0F1): Biochemical and molecular biological approaches. Microbiol Rev 47:285–312Google Scholar
  7. Gebhardt NA, Thauer RK, Linder D, Kaulfers P-M, Pfennig N (1985) Mechanism of acetate oxidation to CO2 with elemental sulfur in Desulfuromonas acetoxidans. Arch Microbiol 141: 392–398Google Scholar
  8. King TE, Morris RO (1967) Determination of acid-labile sulfide and sulfhydryl groups. In: Estabrook RW, Pullman ME (eds) Methods in enzymology, vol X. Academic Press, New York San Francisco London, pp 634–641Google Scholar
  9. Klingenberg M, Schollmeyer P (1960) Zur Reversibilität der oxydativen Phosphorylierung. Adenosintriphosphat-abhängige Atmungskontrolle und Reduktion von Diphosphopyridin-nucleotid in Mitochondrien. Biochem Z 333:335–350Google Scholar
  10. Kröger A (1974) Electron-transport phosphorylation coupled to fumarate reduction in anaerobically grown Proteus rettgeri. Biochim Biophys Acta 347:273–289Google Scholar
  11. Kröger A, Innerhofer A (1976) The function of menaquinone, covalently bound FAD and iron-sulfur protein in the electron transport from formate to fumarate of Vibrio succinogenes. Eur J Biochem 69:487–495Google Scholar
  12. Kröger A, Winkler E, Innerhofer A, Hackenberg H, Schägger H (1979) The formate dehydrogenase involved in electron transport from formate to fumarate in Vibrio succinogenes. Eur J Biochem 94:465–475Google Scholar
  13. Kruber O (1929) Über das 2,3-Dimethyl-naphthalin im Steinkohlenteer. Ber Deutsche Chem Ges, pp 3044–3046Google Scholar
  14. Pfennig N, Biebl H (1976) Desulfuromonas acetoxidans gen. nov. and sp. nov., a new anaerobic, sulfur-reducing, acetate-oxidizing bacterium. Arch Microbiol 110:3–12Google Scholar
  15. Pfennig N, Widdel F (1981) Ecology and physiology of some anaerobic bacteria from the microbial sulfur cycle. In: Bothe H, Trebst A (eds) Biology of inorganic nitrogen and sulfur. Springer, Berlin Heidelberg New York, pp 169–177Google Scholar
  16. Solioz M (1984) Dicyclohexylcarbodiimide as a probe for proton translocating enzymes. TIBS 9:309–312Google Scholar
  17. Thauer RK, Morris JG (1984) Metabolism of chemotrophic anaerobes: old views and new aspects. In: Kelly DP, Carr NG (eds) The microbe 1984. Part II. Procaryotes and eukaryotes. Soc Gen Microbiol Symposium 36, Cambridge University Press, pp 123–168Google Scholar
  18. Thauer RK, Jungermann K, Decker K (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41:100–180Google Scholar
  19. Vogel G, Steinhart R (1976) ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunits. Biochemistry 15:208–216Google Scholar

Copyright information

© Springer-Verag 1986

Authors and Affiliations

  • Jens Paulsen
    • 1
  • Achim Kröger
    • 1
  • Rudolf K. Thauer
    • 1
  1. 1.Fachbereich Biologie der UniversitätMarburgGermany

Personalised recommendations