## 4-Thioflavins as active site probes of flavoproteins : reactions with sulfite

1984
Biemann, Monika
Claiborne, Al
Massey, Vincent
Journal article
##### Published in
Journal of Biological Chemistry ; 259 (1984), 21. - pp. 13355-13362. - ISSN 0021-9258. - eISSN 1083-351X
##### Abstract
4-Thioflavins react with sulfite under aerobic conditions to yield highly fluorescent products with absorption maxima aroun 410 nm. These producths have been identified as 4-hydroxy-4-sulfonylflavins, and have been shown to arise from a series of reactions following the O2-dependent reoxidation of an intermediate with absorption maxima at 363 and 465 nm. Under anaerobic conditions, the same intermediate is formed, but decays to a 350 nm absorbing species, which is probably the N(5)-sulfite adduct of 4-thioflavin. A plausible mechanism is described for the formation of the derivatives, and several of their chemical and physical properties are described. Distinctly different results between different proteins are obtained when sulfite reacts with enzyme-bound 4-thioflavins. 4-Thio-FAD-D-amino acid oxidase and 4-thio-FMN-lactate oxidase react rapidly to yield the N(5)-sulfite adducts, as occurs with the native enzymes. 4-Thio- FAD-p-hydroxybenzoate hydroxylase reacts slowly in a manner paralleling the reaction with the free 4- thioflavins.
##### Subject (DDC)
570 Biosciences, Biology
##### Cite This
ISO 690BIEMANN, Monika, Al CLAIBORNE, Sandro GHISLA, Vincent MASSEY, 1984. 4-Thioflavins as active site probes of flavoproteins : reactions with sulfite. In: Journal of Biological Chemistry. 259(21), pp. 13355-13362. ISSN 0021-9258. eISSN 1083-351X
BibTex
@article{Biemann19844Thio-6902,
year={1984},
title={4-Thioflavins as active site probes of flavoproteins : reactions with sulfite},
number={21},
volume={259},
issn={0021-9258},
journal={Journal of Biological Chemistry},
pages={13355--13362},
author={Biemann, Monika and Claiborne, Al and Ghisla, Sandro and Massey, Vincent}
}

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#" >
<bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6902"/>
<dc:format>application/pdf</dc:format>
<dc:contributor>Claiborne, Al</dc:contributor>
<dc:creator>Massey, Vincent</dc:creator>
<dcterms:title>4-Thioflavins as active site probes of flavoproteins : reactions with sulfite</dcterms:title>
<dc:contributor>Massey, Vincent</dc:contributor>
<dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6902/1/4_Thioflavins_as_active_site_probes_of_flavoproteins_reactions.pdf"/>
<dc:creator>Ghisla, Sandro</dc:creator>
<dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dc:creator>Biemann, Monika</dc:creator>
<dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:01Z</dc:date>
<dc:contributor>Ghisla, Sandro</dc:contributor>
<dc:language>eng</dc:language>
<dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:01Z</dcterms:available>
<dc:creator>Claiborne, Al</dc:creator>
<dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 259 (1984), 21, pp. 13355-13362</dcterms:bibliographicCitation>
<dcterms:abstract xml:lang="eng">4-Thioflavins react with sulfite under aerobic conditions to yield highly fluorescent products with absorption maxima aroun 410 nm. These producths have been identified as 4-hydroxy-4-sulfonylflavins, and have been shown to arise from a series of reactions following the O2-dependent reoxidation of an intermediate with absorption maxima at 363 and 465 nm. Under anaerobic conditions, the same intermediate is formed, but decays to a 350 nm absorbing species, which is probably the N(5)-sulfite adduct of 4-thioflavin. A plausible mechanism is described for the formation of the derivatives, and several of their chemical and physical properties are described. Distinctly different results between different proteins are obtained when sulfite reacts with enzyme-bound 4-thioflavins. 4-Thio-FAD-D-amino acid oxidase and 4-thio-FMN-lactate oxidase react rapidly to yield the N(5)-sulfite adducts, as occurs with the native enzymes. 4-Thio- FAD-p-hydroxybenzoate hydroxylase reacts slowly in a manner paralleling the reaction with the free 4- thioflavins.</dcterms:abstract>