Bacterial respiration of arsenic and selenium

FEMS Microbiol Rev. 1999 Oct;23(5):615-27. doi: 10.1111/j.1574-6976.1999.tb00416.x.

Abstract

Oxyanions of arsenic and selenium can be used in microbial anaerobic respiration as terminal electron acceptors. The detection of arsenate and selenate respiring bacteria in numerous pristine and contaminated environments and their rapid appearance in enrichment culture suggest that they are widespread and metabolically active in nature. Although the bacterial species that have been isolated and characterized are still few in number, they are scattered throughout the bacterial domain and include Gram-positive bacteria, beta, gamma and epsilon Proteobacteria and the sole member of a deeply branching lineage of the bacteria, Chrysiogenes arsenatus. The oxidation of a number of organic substrates (i.e. acetate, lactate, pyruvate, glycerol, ethanol) or hydrogen can be coupled to the reduction of arsenate and selenate, but the actual donor used varies from species to species. Both periplasmic and membrane-associated arsenate and selenate reductases have been characterized. Although the number of subunits and molecular masses differs, they all contain molybdenum. The extent of the environmental impact on the transformation and mobilization of arsenic and selenium by microbial dissimilatory processes is only now being fully appreciated.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Arsenic / metabolism*
  • Arsenite Transporting ATPases
  • Bacteria / enzymology*
  • DNA, Bacterial / genetics
  • DNA, Ribosomal / genetics
  • Ion Pumps*
  • Membrane Proteins / metabolism
  • Multienzyme Complexes*
  • Oxidoreductases / metabolism
  • RNA, Ribosomal, 16S / analysis
  • Selenium / metabolism*
  • Selenium / toxicity

Substances

  • DNA, Bacterial
  • DNA, Ribosomal
  • Ion Pumps
  • Membrane Proteins
  • Multienzyme Complexes
  • RNA, Ribosomal, 16S
  • Oxidoreductases
  • selenate reductase
  • Adenosine Triphosphatases
  • Arsenite Transporting ATPases
  • Selenium
  • Arsenic