{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Manna P"],"funding":["U.S. Department of Energy","Human Frontier Science Program","Basic Energy Sciences","Chemical Sciences, Geosciences, and Biosciences Division"],"pagination":["3091-3102"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8390968"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(15)"],"pubmed_abstract":["In green plants, light harvesting complex of Photosystem II (LHCII) absorbs and transports excitation energy toward the photosynthetic reaction centers and serves as a site for energy-dependent nonphotochemical quenching (qE), the photoprotective dissipation of energy as heat. LHCII is thought to activate dissipation through conformational changes that change the photophysical behaviors. Understanding this balance requires a characterization of how the conformations of LHCII, and thus its photophysics, are influenced by individual factors within the membrane environment. Here, we used ensemble and single-molecule fluorescence to characterize the excited-state lifetimes and switching kinetics of LHCII embedded in nanodisc- and liposome-based model membranes of various sizes and lipid compos"],"journal":["Biophysical journal"],"pubmed_title":["Membrane-dependent heterogeneity of LHCII characterized using single-molecule spectroscopy."],"pmcid":["PMC8390968"],"funding_grant_id":["RGY0076","DE-SC0018097"],"pubmed_authors":["Johnson MP","Manna P","Hoffmann M","Schlau-Cohen GS","Davies T"],"additional_accession":[]},"is_claimable":false,"name":"Membrane-dependent heterogeneity of LHCII characterized using single-molecule spectroscopy.","description":"In green plants, light harvesting complex of Photosystem II (LHCII) absorbs and transports excitation energy toward the photosynthetic reaction centers and serves as a site for energy-dependent nonphotochemical quenching (qE), the photoprotective dissipation of energy as heat. LHCII is thought to activate dissipation through conformational changes that change the photophysical behaviors. Understanding this balance requires a characterization of how the conformations of LHCII, and thus its photophysics, are influenced by individual factors within the membrane environment. Here, we used ensemble and single-molecule fluorescence to characterize the excited-state lifetimes and switching kinetics of LHCII embedded in nanodisc- and liposome-based model membranes of various sizes and lipid compos","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Aug","modification":"2026-06-01T02:18:34.789Z","creation":"2025-04-05T23:23:00.025Z"},"accession":"S-EPMC8390968","cross_references":{"pubmed":["34214527"],"doi":["10.1016/j.bpj.2021.06.010"]}}