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Mechanism of bacterial bioluminescence : 4a,5-Dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics

Mechanism of bacterial bioluminescence : 4a,5-Dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics

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ECKSTEIN, Jens W., J. Woodland HASTINGS, Sandro GHISLA, 1993. Mechanism of bacterial bioluminescence : 4a,5-Dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics. In: Biochemistry. 32(2), pp. 404-411. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi00053a004

@article{Eckstein1993Mecha-8116, title={Mechanism of bacterial bioluminescence : 4a,5-Dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics}, year={1993}, doi={10.1021/bi00053a004}, number={2}, volume={32}, issn={0006-2960}, journal={Biochemistry}, pages={404--411}, author={Eckstein, Jens W. and Hastings, J. Woodland and Ghisla, Sandro} }

<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/rdf/resource/123456789/8116"> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:creator>Ghisla, Sandro</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:40:44Z</dc:date> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:40:44Z</dcterms:available> <dcterms:issued>1993</dcterms:issued> <dc:contributor>Eckstein, Jens W.</dc:contributor> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8116/1/Mechanism_of_bacterial_bioluminescence.pdf"/> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:title>Mechanism of bacterial bioluminescence : 4a,5-Dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics</dcterms:title> <dc:language>eng</dc:language> <dc:creator>Eckstein, Jens W.</dc:creator> <dcterms:abstract xml:lang="eng">Bioluminescence catalyzed by bacterial luciferases was measured using FMN, iso-FMN (6-methyl-8-nor-FMN), and FMN analogs carrying the following substituents at position 8: -H, -Cl, -F, SMe, SOMe, S02Me, or -0Me. The first-order rate constants for the decay of light emission correlate with the one-electron oxidation potentials of the 4a,5-dihydro forms of the FMN analogs. To determine thevalues of these potentials, isoalloxazine (flavin) derivatives having the 4a,5-propano-4a,5-dihydros tructure and -H, -CH3, -C1, -OCH3, and -NH2 as substituents at position 8 have been synthesized as models for the 4a-peroxy-4a,5-dihydroflavin intermediates occurring during catalysis by the flavin-dependent monooxygenase luciferase. The tetrahydropyrrole ring between positions 4a and 5 of these isoalloxazine derivatives stabilizes the 4a,5-dihydroflavin by impeding formation of the thermodynamically more stable 1,5-dihydro form. One-electron oxidation potentials (Eobs) were measured by cyclic voltammetry and used to determine the empirical coefficients in the Swain equation. On the basis of this, the one-electron oxidation potentials of 4a,5-propano-4a,5-dihydraon alogs with other substituents in position 8 were calculated (Ecalc). The bioluminescence reaction rate is fastest with FMN analogs of lowest oxidation potential; Le., the slope of the correlation is negative. This indicates that in the rate-limiting step the 4a,5-dihydroflavin moiety donates negative charge. The results are compatible with an intramolecular, chemically initiated electron exchange luminescence mechanism for the bacterial luciferase reaction. A good correlation was also found between EOba nd the literature values of the 2-electron oxidation/reduction potentials (Eredox) of the couple FIox/1,5-dihydro-FIrf~o r the flavin derivatives having the same substituent at position 8. The effects of the substituent in position 8 on the redox properties of 1,5-dihydro- and 4a,5-dihydroflavins are thus essentially the same. This indicates that the earlier use of readily available redox potentials for FIox/1,5-dihydro-FIred for studying reactions involving the 4aS-dihydro isomer was sound.</dcterms:abstract> <dc:format>application/pdf</dc:format> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Hastings, J. Woodland</dc:creator> <dcterms:bibliographicCitation>First publ. in: Biochemistry ; 32 (1993), 2. - S. 404-411</dcterms:bibliographicCitation> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8116/1/Mechanism_of_bacterial_bioluminescence.pdf"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8116"/> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:contributor>Hastings, J. Woodland</dc:contributor> <dc:rights>deposit-license</dc:rights> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> </rdf:Description> </rdf:RDF>

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