dc.contributor.author | Lehtivuori, Heli | |
dc.contributor.author | Rumfeldt, Jessica | |
dc.contributor.author | Mustalahti, Satu | |
dc.contributor.author | Kurkinen, Sami | |
dc.contributor.author | Takala, Heikki | |
dc.date.accessioned | 2022-08-12T07:04:34Z | |
dc.date.available | 2022-08-12T07:04:34Z | |
dc.date.issued | 2022 | |
dc.identifier.citation | Lehtivuori, H., Rumfeldt, J., Mustalahti, S., Kurkinen, S., & Takala, H. (2022). Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome. <i>Photochemical and Photobiological Sciences</i>, <i>21</i>(11), 1975-1989. <a href="https://doi.org/10.1007/s43630-022-00272-6" target="_blank">https://doi.org/10.1007/s43630-022-00272-6</a> | |
dc.identifier.other | CONVID_150995821 | |
dc.identifier.uri | https://jyx.jyu.fi/handle/123456789/82490 | |
dc.description.abstract | Phytochromes are red light-sensing photoreceptor proteins that bind a bilin chromophore. Here, we investigate the role of a conserved histidine (H260) and tyrosine (Y263) in the chromophore-binding domain (CBD) of Deinococcus radiodurans phytochrome (DrBphP). Using crystallography, we show that in the H260A variant, the missing imidazole side chain leads to increased water content in the binding pocket. On the other hand, Y263F mutation reduces the water occupancy around the chromophore. Together, these changes in water coordination alter the protonation and spectroscopic properties of the biliverdin. These results pinpoint the importance of this conserved histidine and tyrosine, and the related water network, for the function and applications of phytochromes. | en |
dc.format.mimetype | application/pdf | |
dc.language.iso | eng | |
dc.publisher | Springer Science and Business Media LLC | |
dc.relation.ispartofseries | Photochemical and Photobiological Sciences | |
dc.rights | CC BY 4.0 | |
dc.subject.other | fytokromit | |
dc.subject.other | spectral responses | |
dc.subject.other | water network | |
dc.subject.other | biliverdin protonation | |
dc.subject.other | phytochrome structure | |
dc.title | Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome | |
dc.type | article | |
dc.identifier.urn | URN:NBN:fi:jyu-202208124034 | |
dc.contributor.laitos | Bio- ja ympäristötieteiden laitos | fi |
dc.contributor.laitos | Kemian laitos | fi |
dc.contributor.laitos | Fysiikan laitos | fi |
dc.contributor.laitos | Department of Biological and Environmental Science | en |
dc.contributor.laitos | Department of Chemistry | en |
dc.contributor.laitos | Department of Physics | en |
dc.contributor.oppiaine | Solu- ja molekyylibiologia | fi |
dc.contributor.oppiaine | Nanoscience Center | fi |
dc.contributor.oppiaine | Fysikaalinen kemia | fi |
dc.contributor.oppiaine | Fysiikka | fi |
dc.contributor.oppiaine | Cell and Molecular Biology | en |
dc.contributor.oppiaine | Nanoscience Center | en |
dc.contributor.oppiaine | Physical Chemistry | en |
dc.contributor.oppiaine | Physics | en |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | |
dc.type.coar | http://purl.org/coar/resource_type/c_2df8fbb1 | |
dc.description.reviewstatus | peerReviewed | |
dc.format.pagerange | 1975-1989 | |
dc.relation.issn | 1474-905X | |
dc.relation.numberinseries | 11 | |
dc.relation.volume | 21 | |
dc.type.version | publishedVersion | |
dc.rights.copyright | © The Author(s) 2022 | |
dc.rights.accesslevel | openAccess | fi |
dc.relation.grantnumber | 290677 | |
dc.relation.grantnumber | 330678 | |
dc.relation.grantnumber | 277194 | |
dc.subject.yso | valo | |
dc.subject.yso | proteiinit | |
dc.subject.yso | valokemia | |
dc.subject.yso | säteily | |
dc.subject.yso | bakteerit | |
dc.subject.yso | kidetiede | |
dc.subject.yso | fotobiologia | |
dc.subject.yso | spektroskopia | |
dc.format.content | fulltext | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p5742 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p4332 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p7201 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p4150 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p1749 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p643 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p27666 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p10176 | |
dc.rights.url | https://creativecommons.org/licenses/by/4.0/ | |
dc.relation.doi | 10.1007/s43630-022-00272-6 | |
dc.relation.funder | Research Council of Finland | en |
dc.relation.funder | Research Council of Finland | en |
dc.relation.funder | Research Council of Finland | en |
dc.relation.funder | Suomen Akatemia | fi |
dc.relation.funder | Suomen Akatemia | fi |
dc.relation.funder | Suomen Akatemia | fi |
jyx.fundingprogram | Academy Project, AoF | en |
jyx.fundingprogram | Academy Research Fellow, AoF | en |
jyx.fundingprogram | Postdoctoral Researcher, AoF | en |
jyx.fundingprogram | Akatemiahanke, SA | fi |
jyx.fundingprogram | Akatemiatutkija, SA | fi |
jyx.fundingprogram | Tutkijatohtori, SA | fi |
jyx.fundinginformation | This work was supported by Academy of Finland grants 285461 (H.T.), 330678 (H.T., J.R.), 277194 (H.L.), and 290677 (S.M.). | |
dc.type.okm | A1 | |