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dc.contributor.authorFadini, Alisia
dc.contributor.authorHutchison, Christopher D. M.
dc.contributor.authorMorozov, Dmitry
dc.contributor.authorChang, Jeffrey
dc.contributor.authorMaghlaoui, Karim
dc.contributor.authorPerrett, Samuel
dc.contributor.authorLuo, Fangjia
dc.contributor.authorKho, Jeslyn C. X.
dc.contributor.authorRomei, Matthew G.
dc.contributor.authorMorgan, R. Marc L.
dc.contributor.authorOrr, Christian M.
dc.contributor.authorCordon-Preciado, Violeta
dc.contributor.authorFujiwara, Takaaki
dc.contributor.authorNuemket, Nipawan
dc.contributor.authorTosha, Takehiko
dc.contributor.authorTanaka, Rie
dc.contributor.authorOwada, Shigeki
dc.contributor.authorTono, Kensuke
dc.contributor.authorIwata, So
dc.contributor.authorBoxer, Steven G.
dc.contributor.authorGroenhof, Gerrit
dc.contributor.authorNango, Eriko
dc.contributor.authorvan Thor, Jasper J.
dc.date.accessioned2023-07-14T07:05:23Z
dc.date.available2023-07-14T07:05:23Z
dc.date.issued2023
dc.identifier.citationFadini, A., Hutchison, C. D. M., Morozov, D., Chang, J., Maghlaoui, K., Perrett, S., Luo, F., Kho, J. C. X., Romei, M. G., Morgan, R. M. L., Orr, C. M., Cordon-Preciado, V., Fujiwara, T., Nuemket, N., Tosha, T., Tanaka, R., Owada, S., Tono, K., Iwata, S., . . . van Thor, J. J. (2023). Serial Femtosecond Crystallography Reveals that Photoactivation in a Fluorescent Protein Proceeds via the Hula Twist Mechanism. <i>Journal of the American Chemical Society</i>, <i>145</i>(29), 15796-15808. <a href="https://doi.org/10.1021/jacs.3c02313" target="_blank">https://doi.org/10.1021/jacs.3c02313</a>
dc.identifier.otherCONVID_183955250
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/88406
dc.description.abstractChromophore cis/trans photoisomerization is a fundamental process in chemistry and in the activation of many photosensitive proteins. A major task is understanding the effect of the protein environment on the efficiency and direction of this reaction compared to what is observed in the gas and solution phases. In this study, we set out to visualize the hula twist (HT) mechanism in a fluorescent protein, which is hypothesized to be the preferred mechanism in a spatially constrained binding pocket. We use a chlorine substituent to break the twofold symmetry of the embedded phenolic group of the chromophore and unambiguously identify the HT primary photoproduct. Through serial femtosecond crystallography, we then track the photoreaction from femtoseconds to the microsecond regime. We observe signals for the photoisomerization of the chromophore as early as 300 fs, obtaining the first experimental structural evidence of the HT mechanism in a protein on its femtosecond-to-picosecond timescale. We are then able to follow how chromophore isomerization and twisting lead to secondary structure rearrangements of the protein β-barrel across the time window of our measurements.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofseriesJournal of the American Chemical Society
dc.rightsCC BY 4.0
dc.titleSerial Femtosecond Crystallography Reveals that Photoactivation in a Fluorescent Protein Proceeds via the Hula Twist Mechanism
dc.typeresearch article
dc.identifier.urnURN:NBN:fi:jyu-202307144529
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineFysikaalinen kemiafi
dc.contributor.oppiaineNanoscience Centeren
dc.contributor.oppiainePhysical Chemistryen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange15796-15808
dc.relation.issn0002-7863
dc.relation.numberinseries29
dc.relation.volume145
dc.type.versionpublishedVersion
dc.rights.copyright© 2023 The Authors. Published by American Chemical Society
dc.rights.accesslevelopenAccessfi
dc.type.publicationarticle
dc.relation.grantnumber332743
dc.subject.ysoproteiinit
dc.subject.ysofluoresenssi
dc.subject.ysovalokemia
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p3265
jyx.subject.urihttp://www.yso.fi/onto/yso/p7201
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1021/jacs.3c02313
dc.relation.funderResearch Council of Finlanden
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundinginformationThe XFEL experiments were performed at SACLA BL3 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (proposal nos. 2021A8006 and 22019B8021). JJvT and AF acknowledge funding from the Imperial College President’s PhD Scholarship and the Biotechnology and Biological Sciences Research Council (BBSRC) (BB/P00752X/1). GG and DM acknowledge funding from the academy of Finland (grant no. 332743). This work was supported in part by a National Institutes of Health Grant (no. R35GM118044 to SGB). This work was also supported by the Japan Society for the Promotion of Science KAKENHI grants no. 19H05781 (E.N.) and 19H05776 (S. I.); the Platform Project for Supporting Drug Discovery and Life Science Research from the Japan Agency for Medical Research and Development under grant no. JP21am0101070 (S. I.). Use of the Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, is supported by the U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences (contract no. DE-AC02-76SF00515). The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research and by the National Institutes of Health (NIH), National Institute of General Medical Sciences (NIGMS) (including P41GM103393). The contents of this publication are solely the responsibility of the authors and do not necessarily represent the official views of the NIGMS or NIH. We acknowledge TJ Lane for suggestion and discussion on the background subtraction estimation. We also thank Irimpan Matthews for assistance in the data collection at SSRL and acknowledge Diamond Light Source for time on I23 under proposal 23620. The crystallization facility at Imperial College was funded by BBSRC (BB/D524840/1) and the Wellcome Trust (202926/Z/16/Z).
dc.type.okmA1


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