dc.contributor.author | Sauer, PV | |
dc.contributor.author | Cupellini, L | |
dc.contributor.author | Sutter, M | |
dc.contributor.author | Bondanza, M | |
dc.contributor.author | Domínguez Martin, MA | |
dc.contributor.author | Kirst, H | |
dc.contributor.author | Bína, D | |
dc.contributor.author | Koh, AF | |
dc.contributor.author | Kotecha, A | |
dc.contributor.author | Greber, BJ | |
dc.contributor.author | Nogales, E | |
dc.contributor.author | Polívka, T | |
dc.contributor.author | Mennucci, B | |
dc.contributor.author | Kerfeld, CA | |
dc.coverage.spatial | United States | |
dc.date.accessioned | 2024-07-03T12:42:19Z | |
dc.date.available | 2024-07-03T12:42:19Z | |
dc.date.issued | 2024-04-05 | |
dc.identifier | ARTN eadk7535 | |
dc.identifier.citation | Science Advances, 2024, 10 (14), pp. eadk7535 - | en_US |
dc.identifier.issn | 2375-2548 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/6283 | |
dc.identifier.eissn | 2375-2548 | |
dc.identifier.eissn | 2375-2548 | |
dc.identifier.doi | 10.1126/sciadv.adk7535 | |
dc.identifier.doi | 10.1126/sciadv.adk7535 | |
dc.description.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. | |
dc.format | Print-Electronic | |
dc.format.extent | eadk7535 - | |
dc.language | eng | |
dc.language.iso | eng | en_US |
dc.publisher | AMER ASSOC ADVANCEMENT SCIENCE | en_US |
dc.relation.ispartof | Science Advances | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | en_US |
dc.subject | Phycobilisomes | |
dc.subject | Bacterial Proteins | |
dc.subject | Canthaxanthin | |
dc.subject | Cryoelectron Microscopy | |
dc.subject | Cyanobacteria | |
dc.title | Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes. | en_US |
dc.type | Journal Article | |
dcterms.dateAccepted | 2024-03-04 | |
dc.date.updated | 2024-07-03T12:41:14Z | |
rioxxterms.version | VoR | en_US |
rioxxterms.versionofrecord | 10.1126/sciadv.adk7535 | en_US |
rioxxterms.licenseref.startdate | 2024-04-05 | |
rioxxterms.type | Journal Article/Review | en_US |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/38578996 | |
pubs.issue | 14 | |
pubs.organisational-group | ICR | |
pubs.organisational-group | ICR/Primary Group | |
pubs.organisational-group | ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | ICR/Primary Group/ICR Divisions/Structural Biology | |
pubs.organisational-group | ICR/Primary Group/ICR Divisions/Structural Biology/Structural biology of DNA repair complexes | |
pubs.publication-status | Published | |
pubs.publisher-url | http://dx.doi.org/10.1126/sciadv.adk7535 | |
pubs.volume | 10 | |
icr.researchteam | Struct Biol DNA repair | en_US |
dc.contributor.icrauthor | Greber, Basil | |
icr.provenance | Deposited by Mr Arek Surman on 2024-07-03. Deposit type is initial. No. of files: 1. Files: Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes.pdf | |