<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>15(58)</volume><submitter>Merga G</submitter><pubmed_abstract>The function of the biological photoswitch phytochrome is initiated by photoisomerization of the methine-bridged tetrapyrrole chromophore, followed by thermal relaxation steps. As a result of this reaction cascade, the protein interconverts between two parental state. These states, denoted as Pr (red absorbing) and Pfr (far-red absorbing), represent the physiologically inactive and active form of the protein, respectively. In this work we studied the primary photoprocesses of two bacterial phytochromes Agp1 and Agp2, in which either Pr or Pfr is the stable dark state, respectively. We employed cryogenic IR difference and resonance Raman spectroscopy between 4 K and 130 K to trap and characterize the species formed on the reaction pathways from Pfr to Lumi-F in Agp2 and Pr to Lumi-R in Agp1</pubmed_abstract><journal>RSC advances</journal><pagination>49889-49899</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12703697</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Photoisomerization of phytochrome's chromophore: a vibrational spectroscopic view on the primary ground state processes.</pubmed_title><pmcid>PMC12703697</pmcid><pubmed_authors>Ebrahim M</pubmed_authors><pubmed_authors>Große M</pubmed_authors><pubmed_authors>Piwowarski P</pubmed_authors><pubmed_authors>Scheerer P</pubmed_authors><pubmed_authors>Sauthof L</pubmed_authors><pubmed_authors>Hildebrandt P</pubmed_authors><pubmed_authors>Merga G</pubmed_authors><pubmed_authors>Velazquez Escobar F</pubmed_authors><pubmed_authors>Michael N</pubmed_authors><pubmed_authors>Kraskov A</pubmed_authors><pubmed_authors>Bartl F</pubmed_authors></additional><is_claimable>false</is_claimable><name>Photoisomerization of phytochrome's chromophore: a vibrational spectroscopic view on the primary ground state processes.</name><description>The function of the biological photoswitch phytochrome is initiated by photoisomerization of the methine-bridged tetrapyrrole chromophore, followed by thermal relaxation steps. As a result of this reaction cascade, the protein interconverts between two parental state. These states, denoted as Pr (red absorbing) and Pfr (far-red absorbing), represent the physiologically inactive and active form of the protein, respectively. In this work we studied the primary photoprocesses of two bacterial phytochromes Agp1 and Agp2, in which either Pr or Pfr is the stable dark state, respectively. We employed cryogenic IR difference and resonance Raman spectroscopy between 4 K and 130 K to trap and characterize the species formed on the reaction pathways from Pfr to Lumi-F in Agp2 and Pr to Lumi-R in Agp1</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Dec</publication><modification>2026-06-07T05:20:52.522Z</modification><creation>2026-06-07T03:07:03.081Z</creation></dates><accession>S-EPMC12703697</accession><cross_references><pubmed>41403681</pubmed><doi>10.1039/d5ra08731g</doi></cross_references></HashMap>