Molecular radical cations, M •+ , of amino acids and oligopeptides are produced by collision-induced dissociation of mixed complex ions, [Cu II (dien)M] •2+ , that contain Cu II , an amine, typically diethylenetriamine (dien), and the oligopeptide, M. With dien as the amine ligand, abundant M •+ formation is observed only for the amino acids tryptophan and tyrosine, and oligopeptides that contain either the tryptophanyl or tyrosyl residue. Dissociation of the M •+ ion is rich and differs considerably from that of protonated amino acids and peptides. Facile fragmentation occurs around the R-carbon of the tryptophanyl residue. Cleavage of the N-C R bond and proton transfer from the exocyclic methylene group in the side chain to the N-terminal residue results in formation of the [z n -H] •+ ion and elimination of the N-terminal fragment as ammonia or an amide, depending on the position of the tryptophanyl residue. Cleavage of the C R -C bond of an oligopeptide containing a C-terminal tryptophan residue and proton transfer from the carboxylic group to the N-terminal fragment (a carbonyl oxygen atom) results in formation of the [a n + H] •+ ion and elimination of carbon dioxide. Both types of fragmentation have no analogous reactions in protonated peptides. For the M •+ of tryptophanylglycylglycine, WGG, elimination of the tryptophanyl side chain results in GGG •+ . This radical cation fragments by eliminating its C-terminal glycine to give the [b 2 -H] •+ ion, which is an oxazolone and shares much of the structure and reactivity of the b 2 + ion from protonated triglycine. Density functional theory shows the mechanism of forming the [b 2 -H] •+ ion is similar to that of the b 2 + ion, although the free-energy barrier at 29.4 kcal/mol is lower. The [b 2 -H] •+ ion eliminates CO readily to give the [a 2 -H] •+ ion, which is an iminium radical ion.