Biological dehalogenation and halogenation reactions

Chemosphere. 2003 Jul;52(2):299-312. doi: 10.1016/S0045-6535(03)00204-2.

Abstract

A large number of halogenated compounds is produced by chemical synthesis. Some of these compounds are very toxic and cause enormous problems to human health and to the environment. Investigations on the degradation of halocompounds by microorganisms have led to the detection of various dehalogenating enzymes catalyzing the removal of halogen atoms under aerobic and anaerobic conditions involving different mechanisms. On the other hand, more than 3500 halocompounds are known to be produced biologically, some of them in great amounts. Until 1997, only haloperoxidases were thought to be responsible for incorporation of halogen atoms into organic compounds. However, recent investigations into the biosynthesis of halogenated metabolites by bacteria have shown that a novel type of halogenating enzymes, FADH(2)-dependent halogenases, are involved in biosyntheses of halogenated metabolites. In every gene cluster coding for the biosynthesis of a halogenated metabolite, isolated so far, one or several genes for FADH(2)-dependent halogenases have been identified.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacteria / metabolism
  • Biodegradation, Environmental
  • Catalysis
  • Conserved Sequence
  • Enzymes / genetics
  • Enzymes / metabolism
  • Fatty Acid Desaturases
  • Flavin-Adenine Dinucleotide / analogs & derivatives
  • Flavin-Adenine Dinucleotide / metabolism
  • Halogens / chemistry
  • Halogens / metabolism*
  • Hydrocarbons, Halogenated / chemistry
  • Hydrocarbons, Halogenated / metabolism*
  • Oxidation-Reduction
  • Oxidoreductases Acting on CH-CH Group Donors*
  • Sequence Alignment

Substances

  • Enzymes
  • Halogens
  • Hydrocarbons, Halogenated
  • Flavin-Adenine Dinucleotide
  • Fatty Acid Desaturases
  • Oxidoreductases Acting on CH-CH Group Donors
  • 2,4-dienoyl-CoA reductase