Näytä suppeat kuvailutiedot

dc.contributor.authorCellini, Andrea
dc.contributor.authorShankar Madan, Kumar
dc.contributor.authorNimmrich, Amke
dc.contributor.authorHunt Leigh, Anna
dc.contributor.authorMonrroy, Leonardo
dc.contributor.authorMutisya, Jennifer
dc.contributor.authorFurrer, Antonia
dc.contributor.authorBeale, Emma V.
dc.contributor.authorCarrillo, Melissa
dc.contributor.authorMalla Tek, Narsingh
dc.contributor.authorMaj, Piotr
dc.contributor.authorVrhovac, Lidija
dc.contributor.authorDworkowski, Florian
dc.contributor.authorCirelli, Claudio
dc.contributor.authorJohnson, Philip J. M.
dc.contributor.authorOzerov, Dmitry
dc.contributor.authorStojković, Emina A.
dc.contributor.authorHammarström, Leif
dc.contributor.authorBacellar, Camila
dc.contributor.authorStandfuss, Jörg
dc.contributor.authorMaj, Michał
dc.contributor.authorSchmidt, Marius
dc.contributor.authorWeinert, Tobias
dc.contributor.authorIhalainen, Janne A.
dc.contributor.authorWahlgren, Weixiao Yuan
dc.contributor.authorWestenhoff, Sebastian
dc.date.accessioned2024-02-09T13:34:29Z
dc.date.available2024-02-09T13:34:29Z
dc.date.issued2024
dc.identifier.citationCellini, A., Shankar Madan, K., Nimmrich, A., Hunt Leigh, A., Monrroy, L., Mutisya, J., Furrer, A., Beale, E. V., Carrillo, M., Malla Tek, N., Maj, P., Vrhovac, L., Dworkowski, F., Cirelli, C., Johnson, P. J. M., Ozerov, D., Stojković, E. A., Hammarström, L., Bacellar, C., . . . Westenhoff, S. (2024). Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography. <i>Nature Chemistry</i>, <i>Early online</i>. <a href="https://doi.org/10.1038/s41557-023-01413-9" target="_blank">https://doi.org/10.1038/s41557-023-01413-9</a>
dc.identifier.otherCONVID_202860539
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/93321
dc.description.abstractCharge-transfer reactions in proteins are important for life, such as in photolyases which repair DNA, but the role of structural dynamics remains unclear. Here, using femtosecond X-ray crystallography, we report the structural changes that take place while electrons transfer along a chain of four conserved tryptophans in the Drosophila melanogaster (6-4) photolyase. At femto- and picosecond delays, photoreduction of the flavin by the first tryptophan causes directed structural responses at a key asparagine, at a conserved salt bridge, and by rearrangements of nearby water molecules. We detect charge-induced structural changes close to the second tryptophan from 1 ps to 20 ps, identifying a nearby methionine as an active participant in the redox chain, and from 20 ps around the fourth tryptophan. The photolyase undergoes highly directed and carefully timed adaptations of its structure. This questions the validity of the linear solvent response approximation in Marcus theory and indicates that evolution has optimized fast protein fluctuations for optimal charge transfer.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofseriesNature Chemistry
dc.rightsCC BY 4.0
dc.subject.othernanocrystallography
dc.subject.otherphotobiology
dc.titleDirected ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202402091803
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.relation.issn1755-4330
dc.relation.volumeEarly online
dc.type.versionpublishedVersion
dc.rights.copyright© 2024 the Authors
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber332742
dc.subject.ysoDNA
dc.subject.ysoproteiinit
dc.subject.ysofotobiologia
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p7690
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p27666
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1038/s41557-023-01413-9
dc.relation.funderSuomen Akatemiafi
dc.relation.funderResearch Council of Finlanden
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundinginformationS.W. acknowledges the European Research Council for support (grant number 279944). We acknowledge the Paul Scherrer Institute, Villigen, Switzerland, for provision of free-electron laser beamtime at the Alvra instrument of the SwissFEL ARAMIS branch. M.S. acknowledges support by NSF-STC-1231306 (BioXFEL), J.A.I. by the Academy of Finland (grant number 332742), L.H. by the Knut and Alice Wallenberg Foundation (grant number 2019.0071), E.A.S. by the NSF-STC-123306 (BioXFEL) subaward 6227, T.W. by project grant 310030:197674 of the Swiss National Science Foundation and M.C. by the Swiss Nanoscience Institute (grant number 1904). M.K.S. acknowledges Herbert and Karin Jacobson Foundation and Längmanska Kulturfonden (BA23-0489) for funding.
dc.type.okmA1


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