Archives of Microbiology

, Volume 155, Issue 3, pp 238–248

Anaerobic degradation of cresols by denitrifying bacteria

  • Angelika Rudolphi
  • Andreas Tschech
  • Georg Fuchs
Original Papers

DOI: 10.1007/BF00252207

Cite this article as:
Rudolphi, A., Tschech, A. & Fuchs, G. Arch. Microbiol. (1991) 155: 238. doi:10.1007/BF00252207

Abstract

The initial reactions in anaerobic metablism of methylphenols (cresols) and dimethylphenols were studied with denitrifying bacteria. A newly isolated strain, possibly a Paracoccus sp., was able to grow on o-or p-cresol as sole organic substrate with a generation time of 11 h; o-or p-cresol was completely oxidized to CO2 with nitrate being reduced to N2. A denitrifying Pseudomonas-like strain oxidized m-or p-cresol as the sole organic growth substrate completely to CO2 with a generation time of 14 h. Demonstration of intermediates and/or in vitro measurement of enzyme activities suggest the following enzymatic steps:

(1) p-Cresol was metabolized by both strains via benzoyl-CoA as central intermediate as follows: p-cresol → 4-OH-benzaldehyde → 4-OH-benzoate → 4-OH-benzoly-CoA → benzoyl-CoA. Oxidation of the methyl group to 4-OH-benzaldehyde was catalyzed by p-cresol methylhydroxylase. After oxidation of the aldehyde to 4-OH-benzoate, 4-OH-benzoyl-CoA is formed by 4-OH-benzoyl-CoA synthetase; subsequent reductive dehydroxylation of 4-OH-benzoyl-CoA to benzoyl-CoA is catalyzed by 4-OH-benzoyl-CoA reductase (dehydroxylating).

(2) o-Cresol was metabolized in the Paracoccus-like strain via 3-CH3-benzoyl-CoA as central intermediate as follows: o-cresol → 4-OH-3-CH3-benzoate → 4-OH-3-CH3-benzoyl-CoA → 3-CH3-benzoyl-CoA. The following enzymes were demonstrated: (a) An enzyme catalyzing an isototope exchange reaction between 14CO2 and the carboxyl of 4-OH-3-CH3-benzoate; this activity is thought to be a partial reaction catalyzed by an o-cresol carboxylase. (b) 4-OH-3-CH3-benzoyl-CoA synthetase (AMP-forming) activating the carboxylation product 4-OH-3-CH3-benzoate to its coenzyme A thioester. (c) 4-OH-3-CH3-benzoyl-CoA reductase (dehydroxylating) catalyzing the reductive dehydroxylation of the 4-hydroxyl group with reduced benzyl viologen as electron donor to yield 3-CH3-benzoyl-CoA. This thioester may also be formed by action of a coenzyme A ligase when 3-CH3-benzoate is metabolized. 2,4-Dimethylphenol was metabolized via 4-OH-3-CH3-benzoate and further to 3-CH3-benzoyl-CoA.

(3) The initial reactions of anaerobic metabolism of m-cresol in the Pseudomonas-like strain were not resolved. No indication for the oxidation of the methyl group nor for the carboxylation of m-cresol was found. In contrast, 2,4-and 3,4-dimethylphenol were oxidized to 4-OH-3-CH3-and 4-OH-2-CH3-benzoate, respectively, probably initiated by p-cresol methylhydroxylase; however, these compounds were not metabolized further.

Key words

PseudomonasParacoccusCresolsDimethylphenolsp-Cresol methylhydroxylaseo-Cresol carboxylation4-Hydroxy-3-methylbenzoyl-CoA reductase (dehydroxylating)3-Methylbenzoyl-CoAAnaerobic aromatic metabolism

Copyright information

© Springer-Verlag 1991

Authors and Affiliations

  • Angelika Rudolphi
    • 1
  • Andreas Tschech
    • 1
  • Georg Fuchs
    • 1
  1. 1.Abteilung Angewandte MikrobiologieUniversität UlmUlmFederal Republic of Germany
  2. 2.Institut für Mikrobiologie und ImmunologieUniversität UlmUlmFederal Republic of Germany
  3. 3.Department of BiotechnologyLonza Ltd.VispSwitzerland