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Updated: Jun 2, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
Neighboring pyrrolidine amide participation in thioether oxidation. Methionine as a "hopping" site
Richard S Glass1, Christian Schöneich, George S Wilson
1Department of Chemistry and Biochemistry, The University of Arizona, Tucson, Arizona 85721, United States. rglass@u.arizona.edu
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.
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