UV-Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes
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. https://doi.org/10.1111/php.13095
Published inPhotochemistry and Photobiology
© 2019 American Society for Photobiology
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. ...
PublisherWiley-Blackwell Publishing, Inc.
Publication in research information system
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Related funder(s)Jane and Aatos Erkko Foundation; Magnus Ehrnrooth Foundation; Academy of Finland
Funding program(s)Foundation; Academy Project, AoF
Additional information about fundingThe 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.
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