Enzymatic detoxification of cyanide: Clues from Pseudomonas aeruginosa rhodanese

Rita Cipollone, Paolo Ascenzi, Paola Tomao, Francesco Imperi, Paolo Visca

Research output: Contribution to journalArticlepeer-review

Abstract

Cyanide is a dreaded chemical because of its toxic properties. Although cyanide acts as a general metabolic inhibitor, it is synthesized, excreted and metabolized by hundreds of organisms, including bacteria, algae, fungi, plants, and insects, as a mean to avoid predation or competition. Several cyanide compounds are also produced by industrial activities, resulting in serious environmental pollution. Bioremediation has been exploited as a possible alternative to chemical detoxification of cyanide compounds, and various microbial systems allowing cyanide degradation have been described. Enzymatic pathways involving hydrolytic, oxidative, reductive, and substitution/transfer reactions are implicated in detoxification of cyanide by bacteria and fungi. Amongst enzymes involved in transfer reactions, rhodanese catalyzes sulfane sulfur transfer from thiosulfate to cyanide, leading to the formation of the less toxic thiocyanate. Mitochondrial rhodanese has been associated with protection of aerobic respiration from cyanide poisoning. Here, the biochemical and physiological properties of microbial sulfurtransferases are reviewed in the light of the importance of rhodanese in cyanide detoxification by the cyanogenic bacterium Pseudomonas aeruginosa. Critical issues limiting the application of a rhodanese-based cellular system to cyanide bioremediation are also discussed.

Original languageEnglish
Pages (from-to)199-211
Number of pages13
JournalJournal of Molecular Microbiology and Biotechnology
Volume15
Issue number2-3
DOIs
Publication statusPublished - Aug 2008

Keywords

  • Biocatalysis
  • Bioremediation
  • Cyanide
  • Pseudomonas aeruginosa rhodanese
  • Sulfurtransferase

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Microbiology
  • Bioengineering

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