Förster Excitation Energy Transfer in Peridinin-Chlorophyll-a-Protein

Lade...
Vorschaubild
Dateien
39_PCP_biophys_j.pdf
39_PCP_biophys_j.pdfGröße: 170.15 KBDownloads: 432
Datum
2000
Autor:innen
Kleima, Foske J.
Hofmann, Eckhard
Gobets, Bas
Stokkum, Ivo H. M. van
Grondelle, Rienk van
Amerongen, Herbert van
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Biophysical Journal. 2000, 78(1), pp. 344-353. ISSN 0006-3495. eISSN 1542-0086
Zusammenfassung

Time-resolved fluorescence anisotropy spectroscopy has been used to study the chlorophyll a (Chl a) to Chl a excitation energy transfer in the water-soluble peridinin chlorophyll a protein (PCP) of the dinoflagellate Amphidinium carterae. Monomeric PCP binds eight peridinins and two Chl a. The trimeric structure of PCP, resolved at 2 Å (Hofmann et al., 1996, Science. 272:1788 1791), allows accurate calculations of energy transfer times by use of the Förster equation. The anisotropy decay time constants of 6.8 ± 0.8 ps (τ1) and 350 ± 15 ps (τ2) are respectively assigned to intra- and intermonomeric excitation equilibration times. Using the ratio τ1/τ2 and the amplitude of the anisotropy, the best fit of the experimental data is achieved when the Qy transition dipole moment is rotated by 2 7° with respect to the y axis in the plane of the Chl a molecule. In contrast to the conclusion of Moog et al. (1984, Biochemistry. 23:1564 1571) that the refractive index (n) in the Förster equation should be equal to that of the solvent, n can be estimated to be 1.6 ± 0.1, which is larger than that of the solvent (water). Based on our observations we predict that the relatively slow intermonomeric energy transfer in vivo is overruled by faster energy transfer from a PCP monomer to, e.g., the light-harvesting a/c complex.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690KLEIMA, Foske J., Eckhard HOFMANN, Bas GOBETS, Ivo H. M. van STOKKUM, Rienk van GRONDELLE, Kay DIEDERICHS, Herbert van AMERONGEN, 2000. Förster Excitation Energy Transfer in Peridinin-Chlorophyll-a-Protein. In: Biophysical Journal. 2000, 78(1), pp. 344-353. ISSN 0006-3495. eISSN 1542-0086
BibTex
@article{Kleima2000Forst-8660,
  year={2000},
  title={Förster Excitation Energy Transfer in Peridinin-Chlorophyll-a-Protein},
  number={1},
  volume={78},
  issn={0006-3495},
  journal={Biophysical Journal},
  pages={344--353},
  author={Kleima, Foske J. and Hofmann, Eckhard and Gobets, Bas and Stokkum, Ivo H. M. van and Grondelle, Rienk van and Diederichs, Kay and Amerongen, Herbert van}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/8660">
    <dc:creator>Gobets, Bas</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8660"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8660/1/39_PCP_biophys_j.pdf"/>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dcterms:bibliographicCitation>First publ. in: Biophysical Journal 78 (2000), pp. 344-353</dcterms:bibliographicCitation>
    <dc:contributor>Grondelle, Rienk van</dc:contributor>
    <dc:creator>Grondelle, Rienk van</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Amerongen, Herbert van</dc:creator>
    <dc:contributor>Gobets, Bas</dc:contributor>
    <dcterms:issued>2000</dcterms:issued>
    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dc:creator>Hofmann, Eckhard</dc:creator>
    <dc:language>eng</dc:language>
    <dcterms:title>Förster Excitation Energy Transfer in Peridinin-Chlorophyll-a-Protein</dcterms:title>
    <dc:contributor>Stokkum, Ivo H. M. van</dc:contributor>
    <dc:contributor>Hofmann, Eckhard</dc:contributor>
    <dc:contributor>Kleima, Foske J.</dc:contributor>
    <dc:format>application/pdf</dc:format>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8660/1/39_PCP_biophys_j.pdf"/>
    <dcterms:abstract xml:lang="eng">Time-resolved fluorescence anisotropy spectroscopy has been used to study the chlorophyll a (Chl a) to Chl a excitation energy transfer in the water-soluble peridinin chlorophyll a protein (PCP) of the dinoflagellate Amphidinium carterae. Monomeric PCP binds eight peridinins and two Chl a. The trimeric structure of PCP, resolved at 2 Å (Hofmann et al., 1996, Science. 272:1788 1791), allows accurate calculations of energy transfer times by use of the Förster equation. The anisotropy decay time constants of 6.8 ± 0.8 ps (τ1) and 350 ± 15 ps (τ2) are respectively assigned to intra- and intermonomeric excitation equilibration times. Using the ratio τ1/τ2 and the amplitude of the anisotropy, the best fit of the experimental data is achieved when the Qy transition dipole moment is rotated by 2 7° with respect to the y axis in the plane of the Chl a molecule. In contrast to the conclusion of Moog et al. (1984, Biochemistry. 23:1564 1571) that the refractive index (n) in the Förster equation should be equal to that of the solvent, n can be estimated to be 1.6 ± 0.1, which is larger than that of the solvent (water). Based on our observations we predict that the relatively slow intermonomeric energy transfer in vivo is overruled by faster energy transfer from a PCP monomer to, e.g., the light-harvesting a/c complex.</dcterms:abstract>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dc:contributor>Amerongen, Herbert van</dc:contributor>
    <dc:creator>Stokkum, Ivo H. M. van</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:29Z</dcterms:available>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:29Z</dc:date>
    <dc:creator>Diederichs, Kay</dc:creator>
    <dc:creator>Kleima, Foske J.</dc:creator>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen