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Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1 : angular dioxygenation by a three-component enzyme system

Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1 : angular dioxygenation by a three-component enzyme system

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BÜNZ, Patricia V., Alasdair M. COOK, 1993. Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1 : angular dioxygenation by a three-component enzyme system. In: Journal of Bacteriology. 175(20), pp. 6467-6475

@article{Bunz1993Diben-8413, title={Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1 : angular dioxygenation by a three-component enzyme system}, year={1993}, number={20}, volume={175}, journal={Journal of Bacteriology}, pages={6467--6475}, author={Bünz, Patricia V. and Cook, Alasdair M.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8413"> <dc:creator>Cook, Alasdair M.</dc:creator> <dc:language>eng</dc:language> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:rights>deposit-license</dc:rights> <dc:contributor>Bünz, Patricia V.</dc:contributor> <dcterms:title>Dibenzofuran 4,4a-dioxygenase from Sphingomonas sp. strain RW1 : angular dioxygenation by a three-component enzyme system</dcterms:title> <dcterms:bibliographicCitation>First publ. in: Journal of Bacteriology 175 (1993), 20, pp. 6467-6475</dcterms:bibliographicCitation> <dc:format>application/pdf</dc:format> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8413"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:43:24Z</dc:date> <dcterms:abstract xml:lang="eng">Sphingomonas sp. strain RW1 synthesized a constitutive enzyme system that oxygenated dibenzofuran (DBF) to 2,2',3-trihydroxybiphenyl (THB). We purified this dibenzofuran 4,4a-dioxygenase system (DBFDOS) and found it to consist of four components which catalyzed three activities. Two isofunctional, monomeric flavoproteins (components A1 and A2; M(r) of about 44,000) transferred electrons from NADH to the second component (B; M(r) of about 12,000), a ferredoxin, which transported electrons to the heteromultimeric (alpha 2 beta 2) oxygenase component (C; M(r) of alpha, 45,000; M(r) of beta, 23,000). DBFDOS consumed 1 mol each of NADH, O2, and DBF, which was dioxygenated to about 1 mol of THB; no intermediate was observed. The reaction was thus the dioxygenation of DBF at the 4 and 4a positions to give a diene-diol-hemiacetal which rearomatized by spontaneous loss of a phenolate group to form THB. Components A1 and A2 each reduced dichlorophenolindophenol but had negligible activity with cytochrome c; each lost the yellow color, observed to be flavin adenine dinucleotide, upon purification. Component B, which transported electrons to the oxygenase or cytochrome c, had an N-terminal amino acid sequence with high homology to the putidaredoxin of cytochrome P-450cam. The oxygenase had the UV spectrum of a Rieske iron-sulfur center. We presume DBFDOS to be a class IIA dioxygenase system (EC 1.14.12.-), functionally similar to pyrazon dioxygenase.</dcterms:abstract> <dcterms:issued>1993</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:43:24Z</dcterms:available> <dc:creator>Bünz, Patricia V.</dc:creator> <dc:contributor>Cook, Alasdair M.</dc:contributor> </rdf:Description> </rdf:RDF>

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