Photosynthesis Research

, Volume 131, Issue 1, pp 105–117

Ultrafast spectroscopy tracks carotenoid configurations in the orange and red carotenoid proteins from cyanobacteria

  • Václav Šlouf
  • Valentyna Kuznetsova
  • Marcel Fuciman
  • Céline Bourcier de Carbon
  • Adjélé Wilson
  • Diana Kirilovsky
  • Tomáš Polívka
Original Article

DOI: 10.1007/s11120-016-0302-6

Cite this article as:
Šlouf, V., Kuznetsova, V., Fuciman, M. et al. Photosynth Res (2017) 131: 105. doi:10.1007/s11120-016-0302-6

Abstract

A quenching mechanism mediated by the orange carotenoid protein (OCP) is one of the ways cyanobacteria protect themselves against photooxidative stress. Here, we present a femtosecond spectroscopic study comparing OCP and RCP (red carotenoid protein) samples binding different carotenoids. We confirmed significant changes in carotenoid configuration upon OCP activation reported by Leverenz et al. (Science 348:1463–1466. doi: 10.1126/science.aaa7234, 2015) by comparing the transient spectra of OCP and RCP. The most important marker of these changes was the magnitude of the transient signal associated with the carotenoid intramolecular charge-transfer (ICT) state. While OCP with canthaxanthin exhibited a weak ICT signal, it increased significantly for canthaxanthin bound to RCP. On the contrary, a strong ICT signal was recorded in OCP binding echinenone excited at the red edge of the absorption spectrum. Because the carbonyl oxygen responsible for the appearance of the ICT signal is located at the end rings of both carotenoids, the magnitude of the ICT signal can be used to estimate the torsion angles of the end rings. Application of two different excitation wavelengths to study OCP demonstrated that the OCP sample contains two spectroscopically distinct populations, none of which is corresponding to the photoactivated product of OCP.

Keywords

Orange carotenoid protein Red carotenoid protein Non-photochemical quenching Intramolecular charge-transfer state Ultrafast spectroscopy 

Supplementary material

11120_2016_302_MOESM1_ESM.pdf (261 kb)
Supplementary material 1 (PDF 260 kb)

Funding information

Funder NameGrant NumberFunding Note
Grantová Agentura eské Republiky
  • P501/12/G055
Centre National de la Recherche Scientifique

    Copyright information

    © Springer Science+Business Media Dordrecht 2016

    Authors and Affiliations

    1. 1.Institute of Physics and Biophysics, Faculty of ScienceUniversity of South BohemiaČeské BudějoviceCzech Republic
    2. 2.Institute for Integrative Biology of the Cell (I2BC), CEA, CNRSUniversité Paris-Sud, Université Paris-SaclayGif-sur-YvetteFrance
    3. 3.Institut de Biologie et Technologies de Saclay (iBiTec-S)Commissariat à l’Energie Atomique (CEA)Gif-sur-YvetteFrance
    4. 4.Institute of Plant Molecular Biology, Biological CentreCzech Academy of SciencesČeské BudějoviceCzech Republic

    Personalised recommendations