Neighboring pyrrolidine amide participation in thioether oxidation. methionine as a "hopping" site

Richard S. Glass, Christian Schöneich, George S. Wilson, Thomas Nauser, Takuhei Yamamoto, Edward Lorance, Gary S. Nichol, Malika Ammam

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Methionine residues have been shown to function as efficient "hopping" sites in long-range electron transfer in model polyprolyl peptides. We suggest that a key to this ability of methionine is stabilization of the transient sulfur radical cation by neighboring proline amide participation. That is, in a model system a neighboring pyrrolidine amide lowers the oxidation potential of the thioether by over 0.5 V by formation of a two-center three-electron SO bond.

Original languageEnglish (US)
Pages (from-to)2837-2839
Number of pages3
JournalOrganic Letters
Volume13
Issue number11
DOIs
StatePublished - Jun 3 2011

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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    Glass, R. S., Schöneich, C., Wilson, G. S., Nauser, T., Yamamoto, T., Lorance, E., Nichol, G. S., & Ammam, M. (2011). Neighboring pyrrolidine amide participation in thioether oxidation. methionine as a "hopping" site. Organic Letters, 13(11), 2837-2839. https://doi.org/10.1021/ol200793z