A1 Journal article (refereed)
Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome (2022)
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. Photochemical and Photobiological Sciences, 21(11), 1975-1989. https://doi.org/10.1007/s43630-022-00272-6
JYU authors or editors
Publication details
All authors or editors: Lehtivuori, Heli; Rumfeldt, Jessica; Mustalahti, Satu; Kurkinen, Sami; Takala, Heikki
Journal or series: Photochemical and Photobiological Sciences
ISSN: 1474-905X
eISSN: 1474-9092
Publication year: 2022
Publication date: 29/07/2022
Volume: 21
Issue number: 11
Pages range: 1975-1989
Publisher: Springer Science and Business Media LLC
Publication country: Germany
Publication language: English
DOI: https://doi.org/10.1007/s43630-022-00272-6
Publication open access: Openly available
Publication channel open access: Partially open access channel
Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/82490
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.
Keywords: bacteria; proteins; radiation; light (electromagnetic radiation); photochemistry; photobiology; spectroscopy; crystallography
Free keywords: spectral responses; water network; biliverdin protonation; phytochrome structure
Contributing organizations
Related projects
- Phytochrome-based modules – function and applications
- Takala, Heikki
- Research Council of Finland
- Valokytkeytyvien proteiinien primaarirea
- Lehtivuori, Heli
- Research Council of Finland
- Controlling excited state dynamics by surface plasmons
- Groenhof, Gerrit
- Research Council of Finland
Ministry reporting: Yes
VIRTA submission year: 2022
JUFO rating: 1
- Nanoscience Center (Department of Physics PHYS, JYFL) (Faculty of Mathematics and Science) (Department of Chemistry CHEM) (Department of Biological and Environmental Science BIOENV) NSC
- Cell and Molecular Biology (Department of Biological and Environmental Science BIOENV) SMB
- Physical Chemistry (Department of Chemistry CHEM) KEF