Publikation:

A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1

Lade...
Vorschaubild

Datum

1990

Autor:innen

Eckstein, Jens W.
Cho, Ki Woong
Colepicolo, Pio
Hastings, John Woodland
Wilson, Thérèse

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

Biolumineszenz und Blaulichtwahrnehmung
Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Proceedings of the National Academy of Sciences of the United States of America. 1990, 87(4), pp. 1466-1470

Zusammenfassung

Yellow fluorescent protein (YFP), which has a bound FMN, was isolated from the marine bacterium Vibrio fischeri strain Y-1b. Its presence in a luciferase [alkanal monooxygenase (FMN-linked); alkanal, reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing), EC 1.14.14.3] reaction mixture causes a striking color change, and an increase in bioluminescence intensity, as well as a faster rate of intensity decay, so that the quantum yield is not changed. The emission spectrum shows two distinct color bands, one at 490 nm attributed to the unaltered emission of the luciferase system, the other peaking in the yellow around 540 nm due to YFP emission. The kinetics of the two color bands differ, so the spectrum changes with time. The yellow emission reaches its initial maximum intensity later than the blue, and then both blue and yellow emissions decay exponentially with nearly the same pseudo-first-order rate constants, linearly dependent on [YFP] (from 0.01 sec-1 with no YFP to a maximum of ≈0.1 sec-1 at 4°C) but exhibiting a saturation behavior. The data can be interpreted by assuming the interaction of YFP with the peroxyhemiacetal intermediate in the luciferase reaction to form an unstable new complex whose breakdown gives the yellow emitter in its excited state. This simple model fits well the data at [YFP] < 15 µM. The results indicate that a single primary excited state cannot be responsible for the blue and the yellow emissions.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

bacterial luminescence, bacterial luciferase, enzyme mechanism

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690ECKSTEIN, Jens W., Ki Woong CHO, Pio COLEPICOLO, Sandro GHISLA, John Woodland HASTINGS, Thérèse WILSON, 1990. A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1. In: Proceedings of the National Academy of Sciences of the United States of America. 1990, 87(4), pp. 1466-1470
BibTex
@article{Eckstein1990timed-8503,
  year={1990},
  title={A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1},
  number={4},
  volume={87},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  pages={1466--1470},
  author={Eckstein, Jens W. and Cho, Ki Woong and Colepicolo, Pio and Ghisla, Sandro and Hastings, John Woodland and Wilson, Thérèse}
}
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/123456789/8503">
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8503/1/Proc_Natl_Acad_Sci_USA_1990_EcksteinA_time_dependent_bacterial_b.pdf"/>
    <dc:contributor>Hastings, John Woodland</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8503"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8503/1/Proc_Natl_Acad_Sci_USA_1990_EcksteinA_time_dependent_bacterial_b.pdf"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Colepicolo, Pio</dc:contributor>
    <dcterms:title>A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1</dcterms:title>
    <dc:contributor>Cho, Ki Woong</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Eckstein, Jens W.</dc:contributor>
    <dcterms:abstract xml:lang="eng">Yellow fluorescent protein (YFP), which has a bound FMN, was isolated from the marine bacterium Vibrio fischeri strain Y-1b. Its presence in a luciferase [alkanal monooxygenase (FMN-linked); alkanal, reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing), EC 1.14.14.3] reaction mixture causes a striking color change, and an increase in bioluminescence intensity, as well as a faster rate of intensity decay, so that the quantum yield is not changed. The emission spectrum shows two distinct color bands, one at 490 nm attributed to the unaltered emission of the luciferase system, the other peaking in the yellow around 540 nm due to YFP emission. The kinetics of the two color bands differ, so the spectrum changes with time. The yellow emission reaches its initial maximum intensity later than the blue, and then both blue and yellow emissions decay exponentially with nearly the same pseudo-first-order rate constants, linearly dependent on [YFP] (from 0.01 sec-1 with no YFP to a maximum of ≈0.1 sec-1 at 4°C) but exhibiting a saturation behavior. The data can be interpreted by assuming the interaction of YFP with the peroxyhemiacetal intermediate in the luciferase reaction to form an unstable new complex whose breakdown gives the yellow emitter in its excited state. This simple model fits well the data at [YFP] &lt; 15 µM. The results indicate that a single primary excited state cannot be responsible for the blue and the yellow emissions.</dcterms:abstract>
    <dc:contributor>Wilson, Thérèse</dc:contributor>
    <dc:format>application/pdf</dc:format>
    <dc:creator>Ghisla, Sandro</dc:creator>
    <dc:language>eng</dc:language>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:bibliographicCitation>First publ. in: Proceedings of the National Academy of Sciences of the United States of America ; 87 (1990), 4. - S. 1466-1470</dcterms:bibliographicCitation>
    <dc:creator>Wilson, Thérèse</dc:creator>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:44:12Z</dc:date>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:44:12Z</dcterms:available>
    <dcterms:issued>1990</dcterms:issued>
    <dc:creator>Colepicolo, Pio</dc:creator>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:creator>Eckstein, Jens W.</dc:creator>
    <dc:creator>Cho, Ki Woong</dc:creator>
    <dc:creator>Hastings, John Woodland</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