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dc.contributor.authorKübel, Joachim
dc.contributor.authorChenchiliyan, Manoop
dc.contributor.authorOoi, Saik Ann
dc.contributor.authorGustavsson, Emil
dc.contributor.authorIsaksson, Linnéa
dc.contributor.authorKuznetsova, Valentyna
dc.contributor.authorIhalainen, Janne A.
dc.contributor.authorWestenhoff, Sebastian
dc.contributor.authorMaj, Michał
dc.date.accessioned2020-03-17T05:34:36Z
dc.date.available2020-03-17T05:34:36Z
dc.date.issued2020
dc.identifier.citationKübel, J., Chenchiliyan, M., Ooi, S. A., Gustavsson, E., Isaksson, L., Kuznetsova, V., Ihalainen, J. A., Westenhoff, S., & Maj, M. (2020). Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome. <i>Physical Chemistry Chemical Physics</i>, <i>22</i>(17), 9195-9203. <a href="https://doi.org/10.1039/c9cp06995j" target="_blank">https://doi.org/10.1039/c9cp06995j</a>
dc.identifier.otherCONVID_34973592
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/68197
dc.description.abstractPhytochromes are photosensory proteins in plants, fungi, and bacteria, which detect red- and far-red light. They undergo a transition between the resting (Pr) and photoactivated (Pfr) states. In bacterial phytochromes, the Pr-to-Pfr transition is facilitated by two intermediate states, called Lumi-R and Meta-R. The molecular structures of the protein in these states are not known and the molecular mechanism of photoconversion is not understood. Here, we apply transient infrared absorption spectroscopy to study the photocycle of the wild-type and Y263F mutant of the phytochrome from Deinococcus radiodurans (DrBphP) from nanoto milliseconds. We identify two sequentially forming Lumi-R states which differ in the local structure surrounding the carbonyl group of the biliverdin D-ring. We also find that the tyrosine at position 263 alters local structure and dynamics around the D-ring and causes an increased rate of Pfr formation. The results shed new light on the mechanism of light-signalling in phytochrome proteinsen
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherRoyal Society of Chemistry
dc.relation.ispartofseriesPhysical Chemistry Chemical Physics
dc.rightsCC BY 4.0
dc.titleTransient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202003172421
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centeren
dc.contributor.oppiaineCell and Molecular Biologyen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange9195-9203
dc.relation.issn1463-9076
dc.relation.numberinseries17
dc.relation.volume22
dc.type.versionpublishedVersion
dc.rights.copyright© the Owner Societies 2020
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber296135
dc.subject.ysoinfrapunasäteily
dc.subject.ysospektroskopia
dc.subject.ysoproteiinit
dc.subject.ysovalokemia
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p7126
jyx.subject.urihttp://www.yso.fi/onto/yso/p10176
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p7201
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1039/c9cp06995j
dc.relation.funderResearch Council of Finlanden
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundinginformationMC acknowledges the grants UPD2018-0271 and UPD2019-0229 from the Wenner-Gren Foundations. SW thanks the Knut and Alice Wallenberg Foundation for an Academy Fellowship. JAI acknowledges the Academy of Finland (296135), Jane and Aatos Erkko foundation, and the Magnus Ehrnrooth foundation.
dc.type.okmA1


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