Pseudoenzymatic dealkylation of alkyltins by biological dithiols

Fernando Porcelli, Doriana Triggiani, Bethany A. Buck-Koehntop, Larry R. Masterson, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


We investigated the time dependence of the degradation of three alkyltin derivatives by a nine amino acid linear peptide (I1LGCWCYLR 9) containing a CXC motif derived from the primary sequence of stannin, a membrane protein involved in alkyltin toxicity. We monitored the reaction kinetics using the intrinsic fluorescence of the tryptophan residue in position 5 of the peptide and found that all of the alkyltins analyzed are progressively degraded to dialkyl derivatives, following a pseudoenzymatic reaction mechanism. The end point of the reactions is the formation of a covalent complex between the disubstituted alkyltin and the peptide cysteines. These data agree with the speciation profiles proposed for polysubstituted alkyltins in the environment and reveal a possible biotic degradation pathway for these toxic compounds.

Original languageEnglish (US)
Pages (from-to)1219-1225
Number of pages7
JournalJournal of Biological Inorganic Chemistry
Issue number8
StatePublished - Nov 2009


  • Alkyltins
  • Fluorescence spectroscopy
  • Kinetics of dealkylation
  • Organotin compounds
  • Stannin

Fingerprint Dive into the research topics of 'Pseudoenzymatic dealkylation of alkyltins by biological dithiols'. Together they form a unique fingerprint.

Cite this