Light- and temperature-dependent dynamics of chromophore and protein structural changes in bathy phytochrome Agp2

dc.contributor.authorMerga, Galaan
dc.contributor.authorLopez, Maria Fernandez
dc.contributor.authorFischer, Paul
dc.contributor.authorPiwowarski, Patrick
dc.contributor.authorNogacz, Żaneta
dc.contributor.authorKraskov, Anastasia
dc.contributor.authorBuhrke, David
dc.contributor.authorEscobar, Francisco Velazquez
dc.contributor.authorMichael, Norbert
dc.contributor.authorSiebert, Friedrich
dc.contributor.authorScheerer, Patrick
dc.contributor.authorBartl, Franz
dc.contributor.authorHildebrandt, Peter
dc.date.accessioned2021-12-30T13:28:50Z
dc.date.available2021-12-30T13:28:50Z
dc.date.issued2021-08-10
dc.description.abstractBacterial phytochromes are sensoric photoreceptors that transform light absorbed by the photosensor core module (PCM) to protein structural changes that eventually lead to the activation of the enzymatic output module. The underlying photoinduced reaction cascade in the PCM starts with the isomerization of the tetrapyrrole chromophore, followed by conformational relaxations, proton transfer steps, and a secondary structure transition of a peptide segment (tongue) that is essential for communicating the signal to the output module. In this work, we employed various static and time-resolved IR and resonance Raman spectroscopic techniques to study the structural and reaction dynamics of the Meta-F intermediate of both the PCM and the full-length (PCM and output module) variant of the bathy phytochrome Agp2 from Agrobacterium fabrum. In both cases, this intermediate represents a branching point of the phototransformation, since it opens an unproductive reaction channel back to the initial state and a productive pathway to the final active state, including the functional protein structural changes. It is shown that the functional quantum yield, i.e. the events of tongue refolding per absorbed photons, is lower by a factor of ca. two than the quantum yield of the primary photochemical process. However, the kinetic data derived from the spectroscopic experiments imply an increased formation of the final active state upon increasing photon flux or elevated temperature under photostationary conditions. Accordingly, the branching mechanism does not only account for the phytochrome's function as a light intensity sensor but may also modulate its temperature sensitivity.en
dc.description.sponsorshipDFG, 221545957, SFB 1078: Protonation Dynamics in Protein Functionen
dc.description.sponsorshipTU Berlin, Open-Access-Mittel – 2021en
dc.identifier.eissn1463-9084
dc.identifier.issn1463-9076
dc.identifier.pmid34612283
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/16028
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-14802
dc.language.isoenen
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.otherlighten
dc.subject.otherproteinen
dc.subject.otherprotonationen
dc.subject.otherphotochemistryen
dc.titleLight- and temperature-dependent dynamics of chromophore and protein structural changes in bathy phytochrome Agp2en
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1039/d1cp02494aen
dcterms.bibliographicCitation.issue33en
dcterms.bibliographicCitation.journaltitlePhysical Chemistry Chemical Physicsen
dcterms.bibliographicCitation.originalpublishernameRoyal Society of Chemistry (RSC)en
dcterms.bibliographicCitation.originalpublisherplaceCambridgeen
dcterms.bibliographicCitation.pageend18205en
dcterms.bibliographicCitation.pagestart18197en
dcterms.bibliographicCitation.volume23en
tub.accessrights.dnbfreeen
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.groupFG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinen

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