Details

Autor(en) / Beteiligte

• Christou, Nina-Eleni
• Apostolopoulou, Virginia
• Melo, Diogo V M
• Ruppert, Matthias
• Fadini, Alisia
• Henkel, Alessandra
• Sprenger, Janina
• Oberthuer, Dominik
• Günther, Sebastian
• Pateras, Anastasios
• Rahmani Mashhour, Aida
• Yefanov, Oleksandr M
• Galchenkova, Marina
• Reinke, Patrick Y A
• Kremling, Viviane
• Scheer, T Emilie S
• Lange, Esther R
• Middendorf, Philipp
• Schubert, Robin
• De Zitter, Elke
• Lumbao-Conradson, Koya
• Herrmann, Jonathan
• Rahighi, Simin
• Kunavar, Ajda
• Beale, Emma V
• Beale, John H
• Cirelli, Claudio
• Johnson, Philip J M
• Dworkowski, Florian
• Ozerov, Dmitry
• Bertrand, Quentin
• Wranik, Maximilian
• Bacellar, Camila
• Bajt, Saša
• Wakatsuki, Soichi
• Sellberg, Jonas A
• Huse, Nils
• Turk, Dušan
• Chapman, Henry N
• Lane, Thomas J

Titel

Time-resolved crystallography captures light-driven DNA repair

Ist Teil von

• Science (American Association for the Advancement of Science), 2023-12, Vol.382 (6674), p.1015-1020

Ort / Verlag

United States: The American Association for the Advancement of Science

Erscheinungsjahr

2023

Link zum Volltext

Quelle

Science Online《科学》周刊

Beschreibungen/Notizen

• Photolyase is an enzyme that uses light to catalyze DNA repair. To capture the reaction intermediates involved in the enzyme's catalytic cycle, we conducted a time-resolved crystallography experiment. We found that photolyase traps the excited state of the active cofactor, flavin adenine dinucleotide (FAD), in a highly bent geometry. This excited state performs electron transfer to damaged DNA, inducing repair. We show that the repair reaction, which involves the lysis of two covalent bonds, occurs through a single-bond intermediate. The transformation of the substrate into product crowds the active site and disrupts hydrogen bonds with the enzyme, resulting in stepwise product release, with the 3' thymine ejected first, followed by the 5' base.