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The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups

The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups

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GÓMEZ-MANZO, Saúl, Alejandra Abigail GONZÁLEZ-VALDEZ, Jesús ORIA-HERNÁNDEZ, Horacio REYES-VIVAS, Roberto ARREGUÍN-ESPINOSA, Peter KRONECK, Martha Elena SOSA-TORRES, Jose E. ESCAMILLA, 2012. The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups. In: FEMS Microbiology Letters. 328(2), pp. 106-113. ISSN 0378-1097. eISSN 1574-6968

@article{Gomez-Manzo2012-03activ-23573, title={The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups}, year={2012}, doi={10.1111/j.1574-6968.2011.02487.x}, number={2}, volume={328}, issn={0378-1097}, journal={FEMS Microbiology Letters}, pages={106--113}, author={Gómez-Manzo, Saúl and González-Valdez, Alejandra Abigail and Oria-Hernández, Jesús and Reyes-Vivas, Horacio and Arreguín-Espinosa, Roberto and Kroneck, Peter and Sosa-Torres, Martha Elena and Escamilla, Jose E.} }

<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/123456789/23573"> <dc:creator>Sosa-Torres, Martha Elena</dc:creator> <dc:contributor>Reyes-Vivas, Horacio</dc:contributor> <dcterms:issued>2012-03</dcterms:issued> <dc:creator>González-Valdez, Alejandra Abigail</dc:creator> <dc:contributor>Gómez-Manzo, Saúl</dc:contributor> <dc:creator>Reyes-Vivas, Horacio</dc:creator> <dc:creator>Escamilla, Jose E.</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-06-18T14:15:45Z</dc:date> <dc:contributor>Oria-Hernández, Jesús</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Sosa-Torres, Martha Elena</dc:contributor> <dc:rights>deposit-license</dc:rights> <dcterms:bibliographicCitation>FEMS Microbiology Letters ; 328 (2012), 2. - S. 106-113</dcterms:bibliographicCitation> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-06-18T14:15:45Z</dcterms:available> <dc:contributor>Arreguín-Espinosa, Roberto</dc:contributor> <dc:contributor>Escamilla, Jose E.</dc:contributor> <dc:creator>Arreguín-Espinosa, Roberto</dc:creator> <dc:creator>Kroneck, Peter</dc:creator> <dc:contributor>González-Valdez, Alejandra Abigail</dc:contributor> <dc:language>eng</dc:language> <dc:contributor>Kroneck, Peter</dc:contributor> <dc:creator>Oria-Hernández, Jesús</dc:creator> <dc:creator>Gómez-Manzo, Saúl</dc:creator> <dcterms:abstract xml:lang="eng">The membrane-bound alcohol dehydrogenase of Gluconacetobacter diazotrophicus contains one pyrroloquinoline quinone moiety (PQQ), one [2Fe-2S] cluster, and four c-type cytochromes. Here, we describe a novel and inactive enzyme. ADHi, similarly to ADHa, is a heterodimer of 72- and 44-kDa subunits and contains the expected prosthetic groups. However, ADHa showed a threefold molecular mass as compared to ADHi. Noteworthy, the PQQ, the [2Fe-2S] and most of the cytochromes in purified ADHi is in the oxidized form, contrasting with ADHa where the PQQ-semiquinone is detected and the [2Fe-2S] cluster as well as the cytochromes c remained fully reduced after purification. Reduction kinetics of the ferricyanide-oxidized enzymes showed that while ADHa was brought back by ethanol to its full reduction state, in ADHi, only one-quarter of the total heme c was reduced. The dithionite-reduced ADHi was largely oxidized by ubiquinone-2, thus indicating that intramolecular electron transfer is not impaired in ADHi. The acidic pH of the medium might be deleterious for the membrane-bound ADH by causing conformational changes leading to changes in the relative orientation of heme groups and shift of corresponding redox potential to higher values. This would hamper electron transfer resulting in the low activity observed in ADHi.</dcterms:abstract> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/23573"/> <dcterms:title>The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups</dcterms:title> </rdf:Description> </rdf:RDF>

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