Site-Specific Photochemistry along a Protonated Peptide Scaffold.

We present a detailed study of the time-dependent photophysics and photochemistry of a known conformation of the two protonated pentapeptides Leu-enkephalin (Tyrosine-Glycine-Glycine-Phenylalanine-Leucine, YGGFL) and its chromophore-swapped analogue FGGYL, carried out under cryo-cooled conditions in the gas phase. Using ultraviolet-infrared (UV-IR) double resonance, we record excited state IR spectra as a function of time delay between UV and IR pulses. We identify unique Tyr OH stretch transitions due to the S state and the vibrationally excited triplet state(s) formed by intersystem crossing, T(v). Photofragment mass spectra are recorded out of the S origin and following UV-IR double resonance. Several competing site-specific fragmentation pathways are discovered involving peptide backbone cleavage, Tyr side chain loss, and N-terminal NH loss mediated by electron transfer. In YGGFL, IR excitation in the S state promotes electron transfer (ET) from the aromatic ring to the N-terminal R-NH group leading to loss of neutral NH. This product channel is missing in FGGYL due to the larger distance for ET from Y(4) to NH. Selective loss of the Tyr side chain occurs out of an excited state process following UV excitation and is further enhanced by IR excitation in S and T(v) states of both YGGFL and FGGYL. Finally, IR excitation in the S or T(v) states fragments the peptide backbone exclusively at amide(4), producing the b cation. We postulate that this selective fragmentation results from intersystem crossing to produce vibrationally excited triplets with enough energy to launch the proton along a proton conduit present in the known starting structure.