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Title: Fine control of chlorophyll-carotenoid interactions defines the functionality of light-harvesting proteins in plants

Abstract

Photosynthetic antenna proteins can be thought of as “programmed solvents”, which bind pigments at specific mutual orientations, thus tuning the overall energetic landscape and ensuring highly efficient light-harvesting. While positioning of chlorophyll cofactors is well understood and rationalized by the principle of an “energy funnel”, the carotenoids still pose many open questions. Particularly, their short excited state lifetime (<25 ps) renders them potential energy sinks able to compete with the reaction centers and drastically undermine light-harvesting efficiency. Exploration of the orientational phase-space revealed that the placement of central carotenoids minimizes their interaction with the nearest chlorophylls in the plant antenna complexes LHCII, CP26, CP29 and LHCI. At the same time we show that this interaction is highly sensitive to structural perturbations, which has a profound effect on the overall lifetime of the complex. This links the protein dynamics to the light-harvesting regulation in plants by the carotenoids.

Authors:
ORCiD logo [1]; ORCiD logo [1];  [2];  [3];  [4]; ORCiD logo [3]; ORCiD logo [1]
  1. Queen Mary Univ. of London (United Kingdom)
  2. Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
  3. Univ. of Pisa (Italy)
  4. Federal Univ. of Lavras (Brazil); Military Inst. of Engineering, Rio de Janeiro (Brazil)
Publication Date:
Research Org.:
Washington Univ., St. Louis, MO (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1500050
Grant/Contract Number:  
SC0001035
Resource Type:
Accepted Manuscript
Journal Name:
Scientific Reports
Additional Journal Information:
Journal Volume: 7; Journal Issue: 1; Journal ID: ISSN 2045-2322
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Balevičius, Vytautas, Fox, Kieran F., Bricker, William P., Jurinovich, Sandro, Prandi, Ingrid G., Mennucci, Benedetta, and Duffy, Christopher D. P. Fine control of chlorophyll-carotenoid interactions defines the functionality of light-harvesting proteins in plants. United States: N. p., 2017. Web. doi:10.1038/s41598-017-13720-6.
Balevičius, Vytautas, Fox, Kieran F., Bricker, William P., Jurinovich, Sandro, Prandi, Ingrid G., Mennucci, Benedetta, & Duffy, Christopher D. P. Fine control of chlorophyll-carotenoid interactions defines the functionality of light-harvesting proteins in plants. United States. doi:10.1038/s41598-017-13720-6.
Balevičius, Vytautas, Fox, Kieran F., Bricker, William P., Jurinovich, Sandro, Prandi, Ingrid G., Mennucci, Benedetta, and Duffy, Christopher D. P. Tue . "Fine control of chlorophyll-carotenoid interactions defines the functionality of light-harvesting proteins in plants". United States. doi:10.1038/s41598-017-13720-6. https://www.osti.gov/servlets/purl/1500050.
@article{osti_1500050,
title = {Fine control of chlorophyll-carotenoid interactions defines the functionality of light-harvesting proteins in plants},
author = {Balevičius, Vytautas and Fox, Kieran F. and Bricker, William P. and Jurinovich, Sandro and Prandi, Ingrid G. and Mennucci, Benedetta and Duffy, Christopher D. P.},
abstractNote = {Photosynthetic antenna proteins can be thought of as “programmed solvents”, which bind pigments at specific mutual orientations, thus tuning the overall energetic landscape and ensuring highly efficient light-harvesting. While positioning of chlorophyll cofactors is well understood and rationalized by the principle of an “energy funnel”, the carotenoids still pose many open questions. Particularly, their short excited state lifetime (<25 ps) renders them potential energy sinks able to compete with the reaction centers and drastically undermine light-harvesting efficiency. Exploration of the orientational phase-space revealed that the placement of central carotenoids minimizes their interaction with the nearest chlorophylls in the plant antenna complexes LHCII, CP26, CP29 and LHCI. At the same time we show that this interaction is highly sensitive to structural perturbations, which has a profound effect on the overall lifetime of the complex. This links the protein dynamics to the light-harvesting regulation in plants by the carotenoids.},
doi = {10.1038/s41598-017-13720-6},
journal = {Scientific Reports},
number = 1,
volume = 7,
place = {United States},
year = {2017},
month = {10}
}

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Works referenced in this record:

Zwischenmolekulare Energiewanderung und Fluoreszenz
journal, January 1948