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Updated: Jul 15, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Ab initio study of the excited-state deactivation pathways of protonated tryptophan and tyrosine
Gilles Grégoire1, Christophe Jouvet, Claude Dedonder
1Laboratoire de Physique des Lasers du CNRS, Institut Galilée, Université Paris 13, 93430 Villetaneuse, France. gregoire@lpl.univ-paris13.fr
Abstract:
In recent experiments, the excited-state lifetimes of protonated aromatic amino acids (TrpH+ and TyrH+) have been recorded by means of pump-probe photodissociation technique. The lifetime of TyrH+ is much longer than that of TrpH+, which has been initially rationalized on the basis of a simple phenomenological model. Besides, specific photofragments including the formation of radical cation after hydrogen loss are observed for TrpH+ that are not found for TyrH+. The ab initio calculations reported here for TrpH+ and TyrH+ using a coupled-cluster method are meant to track the rich photochemistry of these protonated amino acids following UV excitation.
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