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000586311 1001_ $$0P:(DE-H253)PIP1097112$$aChristou, Nina Eleni$$b0
000586311 245__ $$aTime-resolved crystallography captures light-driven DNA repair
000586311 260__ $$aWashington, DC$$bAssoc.$$c2023
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000586311 520__ $$aPhotolyase 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.
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000586311 536__ $$0G:(GEPRIS)194651731$$aDFG project 194651731 - EXC 1074: Hamburger Zentrum für ultraschnelle Beobachtung (CUI): Struktur, Dynamik und Kontrolle von Materie auf atomarer Skala (194651731)$$c194651731$$x3
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000586311 7001_ $$0P:(DE-H253)PIP1093858$$aMelo, Diogo$$b2
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000586311 7001_ $$0P:(DE-H253)PIP1006324$$aChapman, Henry N.$$b38
000586311 7001_ $$0P:(DE-H253)PIP1020283$$aLane, Thomas J.$$b39$$eCorresponding author
000586311 773__ $$0PERI:(DE-600)2089761-3$$a10.1126/science.adj4270$$gVol. 382, no. 6674, p. 1015 - 1020$$n6674$$p1015 - 1020$$tScience / Science now$$v382$$x0036-8075$$y2023
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