A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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. https://doi.org/10.1111/php.13095

JYU-tekijät tai -toimittajat

Rumfeldt, Jessica
Takala, Heikki
Ihalainen, Janne
Liukkonen, Alli

Julkaisun tiedot

Julkaisun kaikki tekijät tai toimittajat: Rumfeldt, Jessica; Takala, Heikki; Liukkonen, Alli; Ihalainen, Janne

Lehti tai sarja: Photochemistry and Photobiology

ISSN: 0031-8655

eISSN: 1751-1097

Julkaisuvuosi: 2019

Volyymi: 95

Lehden numero: 4

Artikkelin sivunumerot: 969-979

Kustantaja: Wiley-Blackwell Publishing, Inc.

Julkaisumaa: Yhdysvallat (USA)

Julkaisun kieli: englanti

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

Julkaisun avoin saatavuus: Ei avoin

Julkaisukanavan avoin saatavuus: 

Julkaisu on rinnakkaistallennettu (JYX): https://jyx.jyu.fi/handle/123456789/65699

Tiivistelmä

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.

YSO-asiasanat: valokemia; proteiinit; bakteerit

Vapaat asiasanat: phytochromes; Deinococcus

Liittyvät organisaatiot

Hankkeet, joissa julkaisu on tehty

OKM-raportointi: Kyllä

Raportointivuosi: 2019

JUFO-taso: 1