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Electron spin resonance evidence for intra- and intermolecular. sigma. sigma. * bonding in methionine radicals: Relative stabilities of S-Cl, S-Br, S-N, and S-S three-electron bonds

Journal Article · · Journal of Physical Chemistry; (United States)
DOI:https://doi.org/10.1021/j100170a020· OSTI ID:7017519

An electron investigation of three-electron {sigma}{sigma}* bond formation in methionine, methionine peptides, and model structures in frozen aqueous solutions is presented. Irradiation of 12 M LiCl or 6.3 M LiBr solutions at 77K results in the Cl{sub 2}{sm bullet}{sup {minus}} and Br{sub 2}{sm bullet}{sup {minus}} radicals, respectively. These species are found to attack the methionine sulfur atom to form halogen adducts. Further annealing results in the more stable intermolecularly bonded disulfide radical adduct, S{sm bullet}{sub +}-S<. Experiments performed to compare the stabilities of the various three-electron bonded species show the following order in increasing stability: >S{sm bullet}-O{sup +}<, Cl{sm bullet}-Cl{sup {minus}}, >S{sm bullet}-Br, >S{sm bullet}{sup +}-NH{sub 2}, >S{sm bullet}{sup +}-S<. UV-vis spectra of the various intermediates taken suggest that the species identified in this work are those identified in previous pulse radiolysis investigations in aqueous solutions at ambient temperatures. Results found for methionine peptides and model structures are similar to those found for methionine with the exception that intramolecular bond formation in the peptides was not a facile. Each of the radical species found are analyzed for hyperfine splitting and g values. Ab initio molecular orbital calculations of optimized geometries and hyperfine splittings and g values. Ab initio molecular orbital calculations of optimized geometries and hyperfine couplings for model compounds for Cl{sm bullet}-S<, >S{sm bullet}{sup +}-NH{sub 2}, and >S{sm bullet}{sup +}-S< bonding are presented. The calculations clearly show the localized {sigma}{sigma}* nature of the bonding and further predict that the S{sm bullet}-N species is stable toward deprotonation from the amine group.

OSTI ID:
7017519
Journal Information:
Journal of Physical Chemistry; (United States), Journal Name: Journal of Physical Chemistry; (United States) Vol. 95:17; ISSN 0022-3654; ISSN JPCHA
Country of Publication:
United States
Language:
English