Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme

Proteomic analysis of secreted membrane vesicles of archaeal Sulfolobus species reveals the presence of endosome sorting complex components

“…Also of interest is the observation that the thiosulfate sulfur transferase, which catalyses the transfer of thiosulfate to sulfur acceptors like cyanide, is present in the membrane vesicle fractions of all three Sulfolobus sp. This protein is believed to protect the respiratory chain from inhibition by cyanide and/or H 2 S and it may not only have a protective role on a cellular level but also at an extracellular level when associated with the vesicles (Billaut-Laden et al 2006). Finally, the vesicles could also be involved in cell adhesion and/or biofilm formation based on the fact that vWA domain proteins are known to play pivotal roles in extracellular matrix formation and cell adhesion (Tuckwell 1999).…”

“…In addition, the membrane vesicles contain a protein homologous to thiosulfate sulfur transferase. These proteins catalyze the transfer of thiosulfate to sulfur acceptors like cyanide, and function in the protection of the respiratory chain from inhibition by cyanide and/or H 2 S (Billaut- Laden et al 2006). Finally, a dipeptide-binding protein (DppA) was identified in these vesicles which together with the S-layer proteins, are the proteins found in all three species that are synthesized as a precursor with a N-terminal signal peptide which directs the protein to the secretion machinery.…”

Pseudomonas aeruginosa, cyanide accumulation and lung function in CF and non-CF bronchiectasis patients

“…However, cyanide (2 mM) has been found to stimulate the respiratory burst of polymorphonucleates upon phagocytosis [42,43], which, if it occurred in the lung during chronic P. aeruginosa infection, may lead to an increased inflammatory response and increased tissue damage. In humans, it is thought that rhodanese (thiosulfate sulfurtransferase) and a-mercaptopyruvate sulfurtransferase contribute to the main pathway for cyanide elimination by converting it to the less toxic thiocyanate [44][45][46].…”

“…Concurrent lung function data were available on all 21 P. aeruginosa-infected CF patients; the group with measurable sputum cyanide (n511) was not different from those without (n510) on the basis of age or sex. However, those with detectable cyanide had significantly poorer lung function than those without (forced expiratory volume in one second (% predicted) 26.8¡3.8 versus 46.0¡6.7%; forced vital capacity (% pred) 44.4¡4.9 versus 60.1¡7.7%).…”

Polymorphic Variants of Human Rhodanese Exhibit Differences in Thermal Stability and Sulfur Transfer Kinetics

“…The TST gene encoding human rhodanese is located on chromosome 22 (16), and two single nucleotide polymorphisms, c.306A3 C and c.853C3 G leading to amino acid substitutions, E102D and P285A, have been reported (17). The allelic frequencies for the single nucleotide polymorphisms in the French Caucasian population are 1% (E102D) and 5% (P285A), respectively.…”