Allyl sulfides are privileged substrates in aqueous cross-metathesis: application to site-selective protein modification

J Am Chem Soc. 2008 Jul 30;130(30):9642-3. doi: 10.1021/ja8026168. Epub 2008 Jul 1.

Abstract

Allyl sulfides undergo efficient cross-metathesis in aqueous media with Hoveyda-Grubbs second generation catalyst 1. The high reactivity of allyl sulfides in cross-metathesis was exploited in the first examples of cross-metathesis on a protein surface. S-Allylcysteine was incorporated chemically into the protein, providing the requisite allyl sulfide handle. Preliminary efforts to genetically incorporate S-allylcysteine into proteins are also reported.

MeSH terms

  • Allyl Compounds / chemistry*
  • Bacillus / enzymology
  • Bacterial Proteins / chemistry*
  • Cysteine / analogs & derivatives
  • Cysteine / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Glucosidases / chemistry
  • Glucosidases / genetics
  • Glucosidases / metabolism
  • Methionine / chemistry
  • Methionine / genetics
  • Methionine / metabolism
  • Models, Molecular
  • Subtilisin / chemistry
  • Sulfides / chemistry*
  • Water / chemistry

Substances

  • Allyl Compounds
  • Bacterial Proteins
  • Sulfides
  • Water
  • allyl sulfide
  • S-allylcysteine
  • Methionine
  • Glucosidases
  • Sulfolobus solfataricus beta-glycosidase
  • Subtilisin
  • Cysteine