Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes-Reference-Cited by-同舟云学术

Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes

Published:2024-04-05 Issue:14 Volume:10 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Sauer Paul V.¹²^ORCID,Cupellini Lorenzo³^ORCID,Sutter Markus⁴⁵⁶^ORCID,Bondanza Mattia³^ORCID,Domínguez Martin María Agustina⁴⁵⁶^ORCID,Kirst Henning⁵⁶^ORCID,Bína David⁷⁸^ORCID,Koh Adrian Fujiet⁹^ORCID,Kotecha Abhay⁹^ORCID,Greber Basil J.¹⁰^ORCID,Nogales Eva¹²⁵¹¹^ORCID,Polívka Tomáš^ORCID,Mennucci Benedetta³^ORCID,Kerfeld Cheryl A.⁴⁵⁶¹²^ORCID

Affiliation:

1. California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA.

2. Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.

3. Dipartimento di Chimica e Chimica Industriale, Università di Pisa, Via G. Moruzzi 13, I-56124 Pisa, Italy.

4. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.

5. Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

6. Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

7. Faculty of Science, University of South Bohemia, Ceske Budejovice, Czech Republic.

8. Biology Centre of the Czech Academy of Sciences, Ceske Budejovice, Czech Republic.

9. Thermo Fisher Scientific, Eindhoven, Netherlands.

10. Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.

11. Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720, USA.

12. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.

Abstract

Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo–electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin’s transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.

Publisher

American Association for the Advancement of Science (AAAS)

Link

https://www.science.org/doi/pdf/10.1126/sciadv.adk7535

Reference56 articles.

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2. Cyanobacterial photoprotection by the orange carotenoid protein

3. Structure, function and evolution of the cyanobacterial orange carotenoid protein and its homologs

4. Structures of a phycobilisome in light-harvesting and photoprotected states

5. Electronic energy transfer in biomacromolecules

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