{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Milrad Y"],"funding":["Alexander von Humboldt Foundation","Deutsche Forschungsgemeinschaft"],"pagination":["kiaf269"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12341890"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["198(4)"],"pubmed_abstract":["Plastocyanin (PC) is a copper-containing protein that acts as a mobile electron carrier in plants during photosynthesis. In this work, we investigated the role of PC phosphorylation in photosynthetic electron transfer, focusing on interactions with both cytochrome b6f (Cytb6f) and photosystem I (PSI) in Chlamydomonas reinhardtii. While the binding and electron transfer between PC and PSI are well characterized, the interaction between PC and Cytf remains less clear. Using chemical cross-linking combined with mass-spectrometry, we identified 2 potential binding models for PC and Cytf: \"side-on\" and \"head-on.\" To evaluate electron transfer, we developed an in vitro system that allowed oxidized PC, formed via light-driven electron transfer at PSI, to reoxidize Cytf. Our data show that a phosp"],"journal":["Plant physiology"],"pubmed_title":["Insights into plastocyanin-cytochrome b6f complex formation: The role of plastocyanin phosphorylation."],"pmcid":["PMC12341890"],"funding_grant_id":["25-1","DFG HI739/13-1/2","1215053","DFG/9-1/-2","DFG FOR 5573/1","1219125"],"pubmed_authors":["Younas M","Hippler M","Scholz M","Milrad Y","Vidal-Meireles A","Wegemann D","Kuhlgert S"],"additional_accession":[]},"is_claimable":false,"name":"Insights into plastocyanin-cytochrome b6f complex formation: The role of plastocyanin phosphorylation.","description":"Plastocyanin (PC) is a copper-containing protein that acts as a mobile electron carrier in plants during photosynthesis. In this work, we investigated the role of PC phosphorylation in photosynthetic electron transfer, focusing on interactions with both cytochrome b6f (Cytb6f) and photosystem I (PSI) in Chlamydomonas reinhardtii. While the binding and electron transfer between PC and PSI are well characterized, the interaction between PC and Cytf remains less clear. Using chemical cross-linking combined with mass-spectrometry, we identified 2 potential binding models for PC and Cytf: \"side-on\" and \"head-on.\" To evaluate electron transfer, we developed an in vitro system that allowed oxidized PC, formed via light-driven electron transfer at PSI, to reoxidize Cytf. Our data show that a phosp","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-04-08T15:50:49.614Z","creation":"2026-04-08T05:38:19.36Z"},"accession":"S-EPMC12341890","cross_references":{"pubmed":["40581738"],"doi":["10.1093/plphys/kiaf269"]}}