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Title: UV Excitation of Carotenoid Binding Proteins OCP and HCP: Excited‐State Dynamics and Product Formation

Journal Article · · ChemPhotoChem
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [3]; ORCiD logo [4];  [2]
  1. Department of Physics Faculty of Science University of South Bohemia Branišovská 1760 370 05 České Budějovice Czech Republic, Department of Physical Chemistry Fritz Haber Institute of the Max Planck Society Faradayweg 4–6 14195 Berlin Germany
  2. Department of Physics Faculty of Science University of South Bohemia Branišovská 1760 370 05 České Budějovice Czech Republic
  3. Environmental Genomics and Systems Biology Molecular Biophysics and Integrated Bioimaging Divisions Lawrence Berkeley National Laboratory Berkeley CA 94720 USA, MSU-DOE Plant Research Laboratory Michigan State University East Lansing MI48824 USA
  4. Environmental Genomics and Systems Biology Molecular Biophysics and Integrated Bioimaging Divisions Lawrence Berkeley National Laboratory Berkeley CA 94720 USA, MSU-DOE Plant Research Laboratory Michigan State University East Lansing MI48824 USA, Department of Biochemistry and Molecular Biology Michigan State University East Lansing MI 48824 USA

Abstract Over the last decade the orange carotenoid protein (OCP) gained attention due to its role in photoprotection in cyanobacteria. Recently, other carotenoid binding proteins such as helical carotenoid proteins (HCPs) have been identified and characterized, although the function of the HCPs is not yet clarified. Here we have examined OCP1 and two HCPs, HCP2 and HCP3, from Tolypothrix PCC 7601 by ultrafast spectroscopy after excitation of both carotenoid canthaxanthin and amino acids tryptophan and tyrosine in UV at 275 nm. We find that the canthaxanthin S 1 lifetime remains the same 3.5 ps as for excitation of the carotenoid S 2 state, but the S* signal is significantly amplified by UV excitation. In contrast to the S 2 excitation, we observe a formation of the canthaxanthin radical cation at 900 nm for all three proteins after 275 nm excitation. In OCP1, UV light also enhances the amplitude of spectral band centered at 550 nm at longer delays. This band likely corresponds to the first photoproduct of the OCP photocycle, suggesting that excess energy excitation and/or direct excitation of amino acids can enhance the product formation.

Sponsoring Organization:
USDOE
OSTI ID:
1828075
Journal Information:
ChemPhotoChem, Journal Name: ChemPhotoChem Vol. 6 Journal Issue: 1; ISSN 2367-0932
Publisher:
Wiley Blackwell (John Wiley & Sons)Copyright Statement
Country of Publication:
Germany
Language:
English

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