A1 Journal article (refereed)
UV-Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes (2019)


Rumfeldt, J., Takala, H., Liukkonen, A., & Ihalainen, J. (2019). UV-Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes. Photochemistry and Photobiology, 95 (4), 969-979. doi:10.1111/php.13095


JYU authors or editors


Publication details

All authors or editors: Rumfeldt, Jessica; Takala, Heikki; Liukkonen, Alli; Ihalainen, Janne

Journal or series: Photochemistry and Photobiology

ISSN: 0031-8655

eISSN: 1751-1097

Publication year: 2019

Volume: 95

Issue number: 4

Pages range: 969-979

Publisher: Wiley-Blackwell Publishing, Inc.

Publication country: United States

Publication language: English

DOI: http://doi.org/10.1111/php.13095

Open Access: Publication channel is not openly available

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/65699


Abstract

Red‐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.


Keywords: photochemistry; proteins; bacteria

Free keywords: phytochromes; Deinococcus


Contributing organizations

Other organizations:


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Ministry reporting: Yes

Reporting Year: 2019

JUFO rating: 1


Last updated on 2020-18-10 at 21:25