Archives of Microbiology

, Volume 181, Issue 3, pp 245–249 | Cite as

Phenyl methyl ethers: novel electron donors for respiratory growth of Desulfitobacterium hafniense and Desulfitobacterium sp. strain PCE-S

  • Anke Neumann
  • Tina Engelmann
  • Roland Schmitz
  • Yvonne Greiser
  • Adelheid Orthaus
  • Gabriele Diekert
Original Paper


Desulfitobacterium hafniense and Desulfitobacterium sp. strain PCE-S grew under anoxic conditions with a variety of phenyl methyl ethers as electron donors in combination with fumarate as electron acceptor. The phenyl methyl ethers were O-demethylated to the corresponding phenol compounds. O-demethylation was strictly dependent on the presence of fumarate; no O-demethylation occurred with CO2 as electron acceptor. One mol phenyl methyl ether R-O-CH3 was O-demethylated to R-OH per 3 mol fumarate reduced to succinate. The growth yields with vanillate or syringate plus fumarate were approximately 15 g cells (dry weight) per mol methyl moiety converted. D. hafniense utilized vanillate or syringate as an electron donor for reductive dehalogenation of 3-Cl-4-hydroxyphenylacetate, whereas strain PCE-S was not able to dechlorinate tetrachloroethene with phenyl methyl ethers. Crude extracts of both organisms showed O-demethylase activity in the O-demethylase assay with vanillate or syringate as substrates when the organism was grown on syringate plus fumarate. Besides the homoacetogenic bacteria, only growing cells of Desulfitobacterium frappieri PCP-1 have thus far been reported to be capable of phenyl methyl ether O-demethylation. This present study is the first report of Desulfitobacteria utilizing phenyl methyl ethers as electron donors for fumarate reduction and for growth.


Desulfitobacterium hafniense Desulfitobacterium sp. strain PCE-S Reductive dehalogenation O-demethylation O-demethylase Phenyl methyl ether Vanillate Syringate Fumarate reduction Dehalorespiration 
















This work was supported by grants from the Deutsche Forschungsgemeinschaft, the EC, and the Fonds der Chemischen Industrie.


  1. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410CrossRefPubMedGoogle Scholar
  2. Blair JA, Saunders KJ (1970) A convenient method for the preparation of d,l-5-methyltetrahydrofolic acid (d,l-5–5,6,7,8-tetrahydropteroyl-l-monoglutamic acid). Anal Biochem 34:376–381PubMedGoogle Scholar
  3. Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254CrossRefPubMedGoogle Scholar
  4. Christiansen N, Ahring BK, Wohlfarth G, Diekert G (1998) Purification and characterization of the 3-chloro-4-hydroxy-phenylacetate reductive dehalogenase of Desulfitobacterium hafniense. FEBS Lett 436:159–62PubMedGoogle Scholar
  5. Dennie D, Gladu I, Le’Pine F, Villemur R, Bisaillon JG, Beaudet R (1998) Spectrum of the reductive dehalogenation activity of Desulfitobacterium frappieri PCP-1. Appl Environ Microbiol 64:4603–4606Google Scholar
  6. Diekert G (1992) The acetogenic bacteria. In: Balows A, Trüper HG, Dworkin M, Harder W, Schleifer KH (eds) The prokaryotes, vol I, Springer, New York, pp 517–533Google Scholar
  7. Engelmann T, Kaufmann F, Diekert G (2001) Isolation and characterization of a veratrol:corrinoid protein methyl transferase from Acetobacterium dehalogenans. Arch Microbiol 175:376–383CrossRefPubMedGoogle Scholar
  8. Gantzer CJ, Wackett LP (1991) Reductive dechlorination catalyzed by bacterial transition-metal coenzymes. Environ Sci Technol 25:715–722Google Scholar
  9. Gerritse J, Drzyzga O, Kloetstra G, Keijmel M, Wiersum LP, Hutson R, Collins MD, Gottschal JC (1999) Influence of different electron donors and acceptors on dehalorespiration of tetrachloroethene by Desulfitobacterium frappieri TCE1. Appl Environ Microbiol 65:5212–5221PubMedGoogle Scholar
  10. Holliger C, Wohlfarth G, Diekert G (1999) Reductive dechlorination in the energy metabolism of anaerobic bacteria. FEMS Microbiol Rev 22:383–398CrossRefGoogle Scholar
  11. Holliger C, Regeard C, Diekert G (2003) Dehalogenation by anaerobic bacteria. In: Dehalogenation: Microbial processes and environmental applications. Häggblom MM, Bossert ID (eds), Kluwer, Norwell, pp 115–157Google Scholar
  12. Kaufmann F, Wohlfarth G, Diekert G (1997) Isolation of O-demethylase, an ether cleaving enzyme system of the homoacetogenic strain MC. Arch Microbiol 168:136–142PubMedGoogle Scholar
  13. Kaufmann F, Wohlfarth G, Diekert G (1998a) O-Demethylase from Acetobacterium dehalogenans. Substrate specificity and function of the participating proteins. Eur J Biochem 253:706–711PubMedGoogle Scholar
  14. Kaufmann F, Wohlfarth G, Diekert G (1998b) O-Demethylase from Acetobacterium dehalogenans. Cloning, sequencing, and active expression of the gene encoding the corrinoid protein. Eur J Biochem 257:515–521PubMedGoogle Scholar
  15. Meßmer M, Reinhardt S, Wohlfarth G, Diekert G (1996) Studies on methyl chloride dehalogenase and O-demethylase in cell extracts of the homoacetogenic strain MC based on a newly developed coupled enzyme assay. Arch Microbiol 165:18–25CrossRefGoogle Scholar
  16. Miller E, Wohlfarth G, Diekert G (1997) Comparative studies on tetrachloroethene reductive dechlorination mediated by Desulfitobacterium sp. strain PCE-S. Arch Microbiol 168:513–519CrossRefPubMedGoogle Scholar
  17. Naidu D, Ragsdale SW (2001) Characterization of a three-component vanillate O-demethylase from Morella thermoacetica. J Bacteriol 183:3276–3281CrossRefPubMedGoogle Scholar
  18. Neumann, A., Siebert, A, Trescher, T., Reinhardt, S., Wohlfarth, G., and Diekert, G. (2002) Tetrachloroethene reductive dehalogenase of Dehalospirillum multivorans: substrate specificity of the native enzyme and its corrinoid cofactor. Arch Microbiol 177:420–426PubMedGoogle Scholar
  19. Wohlfarth G, Diekert G (1997) Anaerobic dehalogenases. Curr Opinion Biotech 8:290–295Google Scholar
  20. Wohlfarth G, Diekert G (1999) Reductive dehalogenases. In: Banerjee R (ed) Chemistry and biochemistry of B12. Wiley, New York, pp 871–893Google Scholar
  21. Wohlfarth G, Geerligs G, Diekert G (1990) Purification and properties of a NADH dependent 5,10-methyltetrahydrofolate reductase from Peptostreptococcus productus. Eur J Biochem 192:411–417PubMedGoogle Scholar
  22. Wohlfarth G, Geerligs G, Diekert G (1991) Purification and characterization of a NADP+-dependent 5,10-methyltetrahydrofolate dehydrogenase from Peptostreptococcus productus Marburg. J Bacteriol 173:1414–1419PubMedGoogle Scholar

Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  • Anke Neumann
    • 2
  • Tina Engelmann
    • 1
  • Roland Schmitz
    • 1
  • Yvonne Greiser
    • 1
  • Adelheid Orthaus
    • 1
  • Gabriele Diekert
    • 1
  1. 1.Institut für MikrobiologieFSU JenaJenaGermany
  2. 2.Engler-Bunte-InstitutUniversität Karlsruhe (TH)KarlsruheGermany

Personalised recommendations