Näytä suppeat kuvailutiedot

dc.contributor.authorRumfeldt, Jessica
dc.contributor.authorTakala, Heikki
dc.contributor.authorLiukkonen, Alli
dc.contributor.authorIhalainen, Janne
dc.date.accessioned2019-10-01T11:06:39Z
dc.date.available2020-03-08T22:35:36Z
dc.date.issued2019
dc.identifier.citationRumfeldt, J., Takala, H., Liukkonen, A., & Ihalainen, J. (2019). UV-Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes. <i>Photochemistry and Photobiology</i>, <i>95</i>(4), 969-979. <a href="https://doi.org/10.1111/php.13095" target="_blank">https://doi.org/10.1111/php.13095</a>
dc.identifier.otherCONVID_28968474
dc.identifier.otherTUTKAID_80946
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/65699
dc.description.abstractRed‐light photosensory proteins, phytochromes, link light activation to biological functions by interconverting between two conformational states. For this, they undergo large‐scale secondary and tertiary changes which follow small‐scale Z to E bond photoisomerization of the covalently bound bilin chromophore. The complex network of amino acid interactions in the chromophore‐binding pocket plays a central role in this process. Highly conserved Y263 and H290 have been found to be important for the photoconversion yield, while H260 has been identified as important for bilin protonation and proton transfer steps. Here, we focus on the roles these amino acids are playing in preserving the chemical properties of bilin in the resting Pr state of the photosensory unit of a bacteriophytochrome from Deinococcus radiodurans. By using pH‐dependent UV‐Vis spectroscopy and spectral decomposition modeling, we confirm the importance of H260 for biliverdin protonation. Further, we demonstrate that in the canonical bacteriophytochromes, the pKa value of the phenol group of the Y263 is uncommonly low. This directly influences the protonation of the bilin molecule and likely the functional properties of the protein. Our study expands the understanding of the tight interplay between the nearby amino acids and bilin in the phytochrome family.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherWiley-Blackwell Publishing, Inc.
dc.relation.ispartofseriesPhotochemistry and Photobiology
dc.rightsIn Copyright
dc.subject.otherphytochromes
dc.subject.otherDeinococcus
dc.titleUV-Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201909254257
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2019-09-25T12:15:13Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange969-979
dc.relation.issn0031-8655
dc.relation.numberinseries4
dc.relation.volume95
dc.type.versionacceptedVersion
dc.rights.copyright© 2019 American Society for Photobiology
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber
dc.relation.grantnumber
dc.relation.grantnumber296135
dc.subject.ysovalokemia
dc.subject.ysobakteerit
dc.subject.ysoproteiinit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p7201
jyx.subject.urihttp://www.yso.fi/onto/yso/p1749
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
dc.rights.urlhttp://rightsstatements.org/page/InC/1.0/?language=en
dc.relation.doi10.1111/php.13095
dc.relation.funderJane ja Aatos Erkon säätiöfi
dc.relation.funderMagnus Ehrnroothin säätiöfi
dc.relation.funderSuomen Akatemiafi
dc.relation.funderJane and Aatos Erkko Foundationen
dc.relation.funderMagnus Ehrnrooth Foundationen
dc.relation.funderResearch Council of Finlanden
jyx.fundingprogramSäätiöfi
jyx.fundingprogramSäätiöfi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramFoundationen
jyx.fundingprogramFoundationen
jyx.fundingprogramAcademy Project, AoFen
jyx.fundinginformationThe research was supported by the Academy of Finland grants 285461 (H.T.), and 296135, Jane and Aatos Erkko foundation, and the Magnus Ehrnrooth foundation (J.A.I). We would like to thank Heikki Häkkänen for assistance with UV-Vis absorption spectroscopy.
dc.type.okmA1


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