Short hydrogen bonds enhance nonaromatic protein-related fluorescence

Stephens, Amberley D.; Qaisrani, Muhammad Nawaz; Ruggiero, Michael T.; Díaz Mirón, Gonzalo; Morzan, Uriel N.; González Lebrero, Mariano C.; Jones, Saul T. E.; Poli, Emiliano; Bond, Andrew D.; Woodhams, Philippa J.; Kleist, Elyse M.; Grisanti, Luca; Gebauer, Ralph; Zeitler, J. Axel; Credgington, Dan; Hassanali, Ali; Kaminski Schierle, Gabriele S. (2021) Short hydrogen bonds enhance nonaromatic protein-related fluorescence. Proceedings of the National Academy of Sciences, 118 (21). ISSN 0027-8424

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Abstract

Fluorescence in biological systems is usually associated with the presence of aromatic groups. Here, by employing a combined experimental and computational approach, we show that specific hydrogen bond networks can significantly affect fluorescence. In particular, we reveal that the single amino acid L-glutamine, by undergoing a chemical transformation leading to the formation of a short hydrogen bond, displays optical properties that are significantly enhanced compared with L-glutamine itself. Ab initio molecular dynamics simulations highlight that these short hydrogen bonds prevent the appearance of a conical intersection between the excited and the ground states and thereby significantly decrease nonradiative transition probabilities. Our findings open the door to the design of new photoactive materials with biophotonic applications.

Item Type:	Article
Uncontrolled Keywords:	short hydrogen bond; intrinsic fluorescence; ultraviolet fluorescence
Subjects:	NATURAL SCIENCES > Physics
Divisions:	Division of Experimental Physics
Depositing User:	Luca Grisanti
Date Deposited:	06 May 2026 13:07
URI:	https://fulir.irb.hr:/id/eprint/11914
DOI:	10.1073/pnas.2020389118

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