Modeling of variant copies of subunit D1 in the structure of photosystem II from Thermosynechococcus elongatus

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dc.contributor.authorLoll, Bernhard
dc.contributor.authorBroser, Matthias
dc.contributor.authorKós, Peter B.
dc.contributor.authorKern, Jan
dc.contributor.authorBiesiadka, Jacek
dc.contributor.authorVass, Imre
dc.contributor.authorSaenger, Wolfram
dc.contributor.authorZouni, Athina
dc.date.accessioned2018-10-01T14:43:59Z
dc.date.available2018-10-01T14:43:59Z
dc.date.issued2008
dc.descriptionDieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG geförderten) Allianz- bzw. Nationallizenz frei zugänglich.de
dc.descriptionThis publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively.en
dc.description.abstractIn the cyanobacterium Thermosynechococcus elongatus BP-1, living in hot springs, the light environment directly regulates expression of genes that encode key components of the photosynthetic multi-subunit protein-pigment complex photosystem II (PSII). Light is not only essential as an energy source to power photosynthesis, but leads to formation of aggressive radicals which induce severe damage of protein subunits and organic cofactors. Photosynthetic organisms develop several protection mechanisms against this photo-damage, such as the differential expression of genes coding for the reaction center subunit D1 in PSII. Testing the expression of the three different genes (psbAI, psbAII, psbAIII) coding for D1 in T. elongatus under culture conditions used for preparing the material used in crystallization of PSII showed that under these conditions only subunit PsbA1 is present. However, exposure to high-light intensity induced partial replacement of PsbA1 with PsbA3. Modeling of the variant amino acids of the three different D1 copies in the 3.0 Å resolution crystal structure of PSII revealed that most of them are in the direct vicinity to redox-active cofactors of the electron transfer chain. Possible structural and mechanistic consequences for electron transfer are discussed.en
dc.description.sponsorshipDFG, SFB 498, Protein-Kofaktor-Wechselwirkungen in biologischen Prozessenen
dc.description.sponsorshipEC/FP6/516510/EU/Linking molecular genetics and bio-mimetic chemistry - a multidisciplinary approach to achieve renewable hydrogen production/SOLAR-Hen
dc.identifier.eissn1437-4315
dc.identifier.issn1431-6730
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/8252
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-7403
dc.language.isoen
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.ddc570 Biowissenschaften; Biologiede
dc.subject.othergene regulationen
dc.subject.otherlight adaptationen
dc.subject.otherphotoprotectionen
dc.subject.otherphotosynthesisen
dc.subject.otherprotein-cofactor interactionen
dc.titleModeling of variant copies of subunit D1 in the structure of photosystem II from Thermosynechococcus elongatusen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1515/BC.2008.058
dcterms.bibliographicCitation.issue5
dcterms.bibliographicCitation.journaltitleBiological chemistryen
dcterms.bibliographicCitation.originalpublishernameDe Gruyteren
dcterms.bibliographicCitation.originalpublisherplaceBerlinen
dcterms.bibliographicCitation.pageend617
dcterms.bibliographicCitation.pagestart609
dcterms.bibliographicCitation.volume389
tub.accessrights.dnbdomain
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinde

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