Physicochemical features of rhodanese: A review

Abstract


Y. Saidu

Rhodanese is a multifunctional, mitochondrial, sulphur transferase that catalyses the detoxification of cyanide by sulphuration in a double displacement (ping pong) mechanistic reaction. It is widely distributed occurring in varieties of plants and animals, where it activity is modulated by a number of factors including differences in species, organs, sex, age and diet. The enzyme is a single polypeptide chain of 289 amino acids with molecular weight of up to 37,000. The active site of rhodanese contains a tryptophanyl residue in close proximity with an essential sulphahydryl group. Many methods for assaying rhodanese have been reported, the most prominent being the one based on the colorimetric estimation of thiocyanate formed from the reaction of cyanide and thiosulphate, catalysed by rhodanese.

Share this article

Awards Nomination

Select your language of interest to view the total content in your interested language

Indexed In
  • Index Copernicus
  • Google Scholar
  • Sherpa Romeo
  • Open J Gate
  • Academic Keys
  • ResearchBible
  • CiteFactor
  • Electronic Journals Library
  • OCLC- WorldCat
  • Universitat Vechta Library
  • Leipzig University Library
  • Max Planck Institute
  • Leibniz Information Centre
  • GEOMAR Library Ocean Research Information Access
  • OPAC
  • WZB
  • ZB MED
  • Bibliothekssystem Universität Hamburg
  • German National Library of Science and Technology
  • Universitat Des Saarlandes Library