Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species

FEBS Lett. 1989 Jul 17;251(1-2):237-40. doi: 10.1016/0014-5793(89)81461-9.

Abstract

The initial reactions in anaerobic degradation of phenol to CO2 have been studied in vitro with a denitrifying Pseudomonas strain grown with phenol and nitrate in the absence of molecular oxygen. Phenol has been proposed to be carboxylated to 4-hydroxybenzoate [(1987) Arch. Microbiol. 148, 213-217]. 4-Hydroxybenzoate was activated to 4-hydroxybenzoyl-CoA by a coenzyme A ligase. Cell extracts also catalyzed the reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA with reduced benzyl viologen as electron donor. This enzyme, benzoyl-CoA:(acceptor) 4-oxidoreductase (hydroxylating) (EC 1.3.99.-), has not been reported before. The data suggest that phenol and 4-hydroxybenzoate are anaerobically metabolized by this strain via benzoyl-CoA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / metabolism*
  • Kinetics
  • Oxidoreductases / metabolism*
  • Oxidoreductases Acting on CH-CH Group Donors*
  • Parabens / metabolism
  • Phenol
  • Phenols / metabolism
  • Pseudomonas / enzymology*

Substances

  • Acyl Coenzyme A
  • Parabens
  • Phenols
  • 4-hydroxybenzoyl-coenzyme A
  • Phenol
  • benzoyl-coenzyme A
  • Oxidoreductases
  • Oxidoreductases Acting on CH-CH Group Donors
  • benzoyl-coenzyme A-4-oxidoreductase
  • 4-hydroxybenzoic acid