Author(s) Zhang, H.; Cao, W.; Yuan, Q.; Zhou, X.; Valiev, M.; Kass, S.R.; Bin Wang, X.
Journal J Phys Chem Lett
Date Published 2020 May 19

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.

DOI 10.1021/acs.jpclett.0c01099
ISSN 1948-7185
Citation J Phys Chem Lett. 2020:43464352.

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