TY  - JOUR
AU  - Christou, Nina Eleni
AU  - Apostolopoulou, Virginia
AU  - Melo, Diogo
AU  - Ruppert, Matthias
AU  - Fadini, Alisia
AU  - Henkel, Alessandra
AU  - Sprenger, Janina
AU  - Oberthuer, Dominik
AU  - Günther, Sebastian
AU  - Pateras, Anastasios
AU  - Rahmani Mashhour, Aida
AU  - Yefanov, Oleksandr M.
AU  - Galchenkova, Marina
AU  - Reinke, Patrick Y. A.
AU  - Kremling, Viviane
AU  - Scheer, T. Emilie S.
AU  - Lange, Esther R.
AU  - Middendorf, Philipp
AU  - Schubert, Robin
AU  - De Zitter, Elke
AU  - Lumbao-Conradson, Koya
AU  - Herrmann, Jonathan
AU  - Rahighi, Simin
AU  - Kunavar, Ajda
AU  - Beale, Emma V.
AU  - Beale, John H.
AU  - Cirelli, Claudio
AU  - Johnson, Philip J. M.
AU  - Dworkowski, Florian
AU  - Ozerov, Dmitry
AU  - Bertrand, Quentin
AU  - Wranik, Maximilian
AU  - Bacellar, Camila
AU  - Bajt, Saša
AU  - Wakatsuki, Soichi
AU  - Sellberg, Jonas A.
AU  - Huse, Nils
AU  - Turk, Dušan
AU  - Chapman, Henry N.
AU  - Lane, Thomas J.
TI  - Time-resolved crystallography captures light-driven DNA repair
JO  - Science / Science now
VL  - 382
IS  - 6674
SN  - 0036-8075
CY  - Washington, DC
PB  - Assoc.
M1  - PUBDB-2023-03865
SP  - 1015 - 1020
PY  - 2023
N1  - ISSN 1095-9203 not unique: **3 hits**. Copyright © 2023 the authors
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:38033070
UR  - <Go to ISI:>//WOS:001243375200004
DO  - DOI:10.1126/science.adj4270
UR  - https://bib-pubdb1.desy.de/record/586311
ER  -