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dc.contributor.authorIhalainen, Janne
dc.contributor.authorGustavsson, Emil
dc.contributor.authorSchröder, Lea
dc.contributor.authorDonnini, Serena
dc.contributor.authorLehtivuori, Heli
dc.contributor.authorIsaksson, Linnéa
dc.contributor.authorThöing, Christian
dc.contributor.authorModi, Vaibhav
dc.contributor.authorBerntsson, Oskar
dc.contributor.authorStucki-Buchli, Brigitte
dc.contributor.authorLiukkonen, Alli
dc.contributor.authorHäkkänen, Heikki
dc.contributor.authorKalenius, Elina
dc.contributor.authorWestenhoff, Sebastian
dc.contributor.authorKottke, Tilman
dc.date.accessioned2018-10-18T06:20:04Z
dc.date.available2019-09-05T21:35:38Z
dc.date.issued2018fi
dc.identifier.citationIhalainen, J., Gustavsson, E., Schröder, L., Donnini, S., Lehtivuori, H., Isaksson, L., . . . Kottke, T. (2018). Chromophore-Protein Interplay During the Phytochrome Photocycle Revealed by Step-Scan FTIR Spectroscopy. <em>Journal of the American Chemical Society</em>, 140 (39), 12396-12404. <a href="https://doi.org/10.1021/jacs.8b04659">doi:10.1021/jacs.8b04659</a>fi
dc.identifier.otherTUTKAID_78793
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/59862
dc.description.abstractPhytochrome proteins regulate many photoresponses of plants and microorganisms. Light absorption causes isomerization of the biliverdin chromophore, which triggers a series of structural changes to activate the signaling domains of the protein. However, the structural changes are elusive, and therefore the molecular mechanism of signal transduction remains poorly understood. Here, we apply two-color step-scan infrared spectroscopy to the bacteriophytochrome from Deinococcus radiodurans. We show by recordings in H2O and D2O that the hydrogen bonds to the biliverdin D-ring carbonyl become disordered in the first intermediate (Lumi-R) forming a dynamic microenvironment, then completely detach in the second intermediate (Meta-R), and finally reform in the signaling state (Pfr). The spectra reveal via isotope labeling that the refolding of the conserved “PHY-tongue” region occurs with the last transition between Meta-R and Pfr. Additional changes in the protein backbone are detected already within microseconds in Lumi-R. Aided by molecular dynamics simulations, we find that a strictly conserved salt bridge between an arginine of the PHY tongue and an aspartate of the chromophore binding domains is broken in Lumi-R and the arginine is recruited to the D-ring C═O. This rationalizes how isomerization of the chromophore is linked to the global structural rearrangement in the sensory receptor. Our findings advance the structural understanding of phytochrome photoactivation.fi
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.relation.ispartofseriesJournal of the American Chemical Society
dc.rightsIn Copyright
dc.subject.otherchromophore-protein interplayfi
dc.subject.otherstep-scan FTIR spectroscopyfi
dc.titleChromophore-Protein Interplay During the Phytochrome Photocycle Revealed by Step-Scan FTIR Spectroscopyfi
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201810034334
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosFysiikan laitosfi
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosThe Department of Biological and Environmental Scienceen
dc.contributor.laitosDepartment of Physicsen
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineSolu- ja molekyylibiologia
dc.contributor.oppiaineFysiikka
dc.contributor.oppiaineOrgaaninen kemia
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2018-10-03T12:15:16Z
dc.description.reviewstatuspeerReviewed
dc.format.pagerange12396-12404
dc.relation.issn0002-7863
dc.relation.numberinseries39
dc.relation.volume140
dc.type.versionacceptedVersion
dc.rights.copyright© 2018 American Chemical Society
dc.rights.accesslevelopenAccessfi
dc.format.contentfulltext
dc.rights.urlhttp://rightsstatements.org/page/InC/1.0/?language=en
dc.relation.doi10.1021/jacs.8b04659


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