Mechanism and energetics of intramolecular hydrogen transfer in amide and peptide radicals and cation-radicals.
Intramolecular hydrogen transfer in five model amide and peptide radicals and cation-radicals was investigated by combined B3LYP-MP2 calculations. Hypervalent ammonium radicals produced by electron capture in protonated peptides undergo competitive elimination of ammonia, H-atom loss, and H-atom migration to neighboring amide carbonyls. The calculated transition state energies for H-atom migration are slightly but uniformly lower than those for H-atom loss. Transition state theory calculations with inclusion of quantum tunneling effects predict k(H migration)/k(H loss) branching ratios that increase with the ring size of the cyclic transition state for the migration. Intramolecular hydrogen-atom migration in amide and peptide radicals can be described by the proton-coupled electron transfer mechanism. The migrating hydrogen atom shows a negligible spin density and substantial positive charge that are typical of a proton migration. Electron transfer occurs through a pi-orbital system and proceeds in the same (clockwise) or opposite (counterclockwise) direction as the proton motion, depending on the electronic properties of the chain connecting the ammonium group and the amide bond.
Turecek
Frantisek
F
Department of Chemistry, Bagley Hall, Box 351700, University of Washington, Seattle, WA 98195-1700, USA.
Syrstad
Erik A
EA
D000409:Alanine / Q000031:analogs & derivatives; D000577:Amides / Q000737:chemistry*; D002412:Cations; D005609:Free Radicals / Q000737:chemistry; D006033:Glycylglycine / Q000031:analogs & derivatives; D006859:Hydrogen / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D013816:Thermodynamics
D000577:Amides; D002412:Cations; D005609:Free Radicals; D010455:Peptides; D006033:Glycylglycine; D006859:Hydrogen; D000409:Alanine