Dresden 2026 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 9: Single Molecule Biophysics
BP 9.6: Vortrag
Montag, 9. März 2026, 18:15–18:30, BAR/0205
Indications for Ultrafast Energy Transfer and Subsequent Disulfide Bond Cleavage in Lysozyme upon Ultrafast Excitation of Aromatic Residues — •Philip Wehling1, Jessica Harich1, Antonia Freibert1, Ru-Pan Wang2, Tae Gyun Woo3, Junho Lee3, Seonghyeon Jeong3, Sungin Yu3, Haneol Oh3, Migel Ochmann1, Victoria Kabanova4, Emma Beale4, Philip Johnson4, Claudio Cirelli4, Camila Bacellar4, Briony Yorke5, Tae Kyu Kim3, and Nils Huse1 — 1University of Hamburg, Hamburg, Germany — 2DESY, Hamburg, Germany — 3KAIST, Daejeon, Republik of Korea — 4Paul Scherrer Institute, Villigen, Switzerland — 5University of Leeds, Leeds, U.K.
Disulfide bonds play a crucial role in stabilizing the tertiary structure of proteins. Ultraviolet (UV) radiation leads to S-S bond cleavage, possibly compromising the functionality of proteins. Femtosecond X-ray absorption spectroscopy at the sulfur K-edge revealed ultrafast geminate disulfide bond reformation in aliphatic disulfides [1]. These findings raise the question how disulfide bridges behave in proteins upon UV irradiation. Disulfide photochemsitry in Lysozyme by UV excitation across the dominant absorption of the aromatic residues leads to efficient sulfur radical formation which must stem from energy transfer. We discuss yields and possible mechanisms of energy transfer in competition with direct photocleavage of disulfide bridges, and implications for energy dissipation and structural integrity of proteins.
[1] M. Ochmann et al, Nat. Commun. 15, 8838 (2024).
Keywords: Energy transfer; Femtosecond X-ray absorption spectroscopy; UV-induced photochemistry; Disulfide bonds; Lysozyme