A1 Journal article (refereed)
Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome (2020)


Kübel, Joachim; Chenchiliyan, Manoop; Ooi, Saik Ann; Gustavsson, Emil; Isaksson, Linnéa; Kuznetsova, Valentyna; Ihalainen, Janne A.; Westenhoff, Sebastian; Maj, Michał (2020). Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome. Physical Chemistry Chemical Physics, 22 (17), 9195-9203. DOI: 10.1039/c9cp06995j


JYU authors or editors


Publication details

All authors or editors: Kübel, Joachim; Chenchiliyan, Manoop; Ooi, Saik Ann; Gustavsson, Emil; Isaksson, Linnéa; Kuznetsova, Valentyna; Ihalainen, Janne A.; Westenhoff, Sebastian; Maj, Michał

Journal or series: Physical Chemistry Chemical Physics

ISSN: 1463-9076

eISSN: 1463-9084

Publication year: 2020

Volume: 22

Issue number: 17

Pages range: 9195-9203

Publisher: Royal Society of Chemistry

Publication country: United Kingdom

Publication language: English

DOI: http://doi.org/10.1039/c9cp06995j

Open Access: Open access publication published in a hybrid channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/68197


Abstract

Phytochromes are photosensory proteins in plants, fungi, and bacteria, which detect red- and far-red light. They undergo a transition between the resting (Pr) and photoactivated (Pfr) states. In bacterial phytochromes, the Pr-to-Pfr transition is facilitated by two intermediate states, called Lumi-R and Meta-R. The molecular structures of the protein in these states are not known and the molecular mechanism of photoconversion is not understood. Here, we apply transient infrared absorption spectroscopy to study the photocycle of the wild-type and Y263F mutant of the phytochrome from Deinococcus radiodurans (DrBphP) from nanoto milliseconds. We identify two sequentially forming Lumi-R states which differ in the local structure surrounding the carbonyl group of the biliverdin D-ring. We also find that the tyrosine at position 263 alters local structure and dynamics around the D-ring and causes an increased rate of Pfr formation. The results shed new light on the mechanism of light-signalling in phytochrome proteins


Keywords: photochemistry; proteins; infrared radiation; spectroscopy


Contributing organizations


Related projects

Biologiset fotosensorit toiminnassa - Ko
Ihalainen, Janne
Academy of Finland
01/09/2016-31/08/2020


Ministry reporting: Yes

Reporting Year: 2020

Preliminary JUFO rating: 2


Last updated on 2020-18-08 at 13:21