This work showcases cryogenic and temperature-dependent "iodide-tagging"photoelectron spectroscopy to probe specific binding sites of amino acids using the glycine-iodide complex (Gly·I-) as a case study. Multiple Gly·I- isomers were generated from ambient electrospray ionization and kinetically isolated in a cryogenic ion trap. These structures were characterized with temperature-dependent "iodide-tagging"negative ion photoelectron spectroscopy (NIPES), where iodide was used as the "messenger"to interpret electronic energetics and structural information of various Gly·I- isomers. Accompanied by theoretical computations and Franck-Condon simulations, a total of five cluster structures have been identified along with their various binding motifs. This work demonstrates that "iodide-tagging"NIPES is a powerful general means for probing specific binding interactions in biological molecules of interest.
PubMed: MeSH publication types
- Journal Article