<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Caspy I</submitter><funding>German-Israeli Foundation for Scientific Research and Development</funding><funding>Israel Science Foundation</funding><funding>NIGMS NIH HHS</funding><pagination>1380</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8660910</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>4(1)</volume><pubmed_abstract>Water molecules play a pivotal functional role in photosynthesis, primarily as the substrate for Photosystem II (PSII). However, their importance and contribution to Photosystem I (PSI) activity remains obscure. Using a high-resolution cryogenic electron microscopy (cryo-EM) PSI structure from a Chlamydomonas reinhardtii temperature-sensitive photoautotrophic PSII mutant (TSP4), a conserved network of water molecules - dating back to cyanobacteria - was uncovered, mainly in the vicinity of the electron transport chain (ETC). The high-resolution structure illustrated that the water molecules served as a ligand in every chlorophyll that was missing a fifth magnesium coordination in the PSI core and in the light-harvesting complexes (LHC). The asymmetric distribution of the water molecules ne</pubmed_abstract><journal>Communications biology</journal><pubmed_title>Dimeric and high-resolution structures of Chlamydomonas Photosystem I from a temperature-sensitive Photosystem II mutant.</pubmed_title><pmcid>PMC8660910</pmcid><funding_grant_id>R01 GM129325</funding_grant_id><funding_grant_id>569/17</funding_grant_id><funding_grant_id>P41 GM103311</funding_grant_id><funding_grant_id>G-1483-207/2018</funding_grant_id><pubmed_authors>Schwartz T</pubmed_authors><pubmed_authors>Fadeeva M</pubmed_authors><pubmed_authors>Caspy I</pubmed_authors><pubmed_authors>Ben-Tal N</pubmed_authors><pubmed_authors>Kessel A</pubmed_authors><pubmed_authors>Bayro-Kaiser V</pubmed_authors><pubmed_authors>Nelson N</pubmed_authors></additional><is_claimable>false</is_claimable><name>Dimeric and high-resolution structures of Chlamydomonas Photosystem I from a temperature-sensitive Photosystem II mutant.</name><description>Water molecules play a pivotal functional role in photosynthesis, primarily as the substrate for Photosystem II (PSII). However, their importance and contribution to Photosystem I (PSI) activity remains obscure. Using a high-resolution cryogenic electron microscopy (cryo-EM) PSI structure from a Chlamydomonas reinhardtii temperature-sensitive photoautotrophic PSII mutant (TSP4), a conserved network of water molecules - dating back to cyanobacteria - was uncovered, mainly in the vicinity of the electron transport chain (ETC). The high-resolution structure illustrated that the water molecules served as a ligand in every chlorophyll that was missing a fifth magnesium coordination in the PSI core and in the light-harvesting complexes (LHC). The asymmetric distribution of the water molecules ne</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Dec</publication><modification>2026-05-31T07:09:13.632Z</modification><creation>2025-04-04T07:57:23.694Z</creation></dates><accession>S-EPMC8660910</accession><cross_references><pubmed>34887518</pubmed><doi>10.1038/s42003-021-02911-7</doi></cross_references></HashMap>