ArticleNature communications2024
UV photochemistry of the L-cystine disulfide bridge in aqueous solution investigated by femtosecond X-ray absorption spectroscopy.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Ultrafast Photodissociation and Recombination Dynamics of MethylACS omega · 2026Article
- Demonstration of time-resolved Fe K-edge XANES with a self-seeded X-ray free-electron laser at PAL-XFEL.Scientific reports · 2025Article
- Light-driven biosensor for the rapid and selective detection of hypoxia-inducible factor-prolyl hydroxylase domain inhibitors in aqueous media and saliva.Mikrochimica acta · 2025Article
- Size-Dependent Ultrafast UV Photochemistry of Aliphatic Disulfides in Solution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
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Authors and funding
15 authors.
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Abstract
The photolysis of disulfide bonds is implicated in denaturation of proteins exposed to ultraviolet light. Despite this biological relevance in stabilizing the structure of many proteins, the mechanisms of disulfide photolysis are still contested after decades of research. Herein, we report new insight into the photochemistry of L-cystine in aqueous solution by femtosecond X-ray absorption spectroscopy at the sulfur K-edge. We observe homolytic bond cleavage upon ultraviolet irradiation and the formation of thiyl radicals as the single primary photoproduct. Ultrafast thiyl decay due to geminate recombination proceeds at a quantum yield of >80 % within 20 ps. These dynamics coincide with the emergence of a secondary product, attributed to the generation of perthiyl radicals. From these findings, we suggest a mechanism of perthiyl radical generation from a vibrationally excited parent molecule that asymmetrically fragments along a carbon-sulfur bond. Our results point toward a dynamic photostability of the disulfide bridge in condensed-phase.
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