Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium

Friedrich, Michael; Schink, Bernhard

Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium

Dateien

1993_Friedrich_233_240.pdfGröße: 949.85 KBDownloads: 257

Datum

1993

Autor:innen

Friedrich, Michael

Schink, Bernhard

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

FEBS European Journal of Biochemistry. 1993, 217(1), pp. 233-240. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1993.tb18238.x

Zusammenfassung

Oxidation of glycolate to 2 CO, and 3 H, (AGO' = +36 kJ/mol glycolate) by the proton-reducing, glycolate-fermenting partner bacterium of a syntrophic coculture (strain FlGlyM) depends on a low hydrogen partial pressure (pH). The first reaction, glycolate oxidation to glyoxylate ( E O f = -92 mV) with protons as electron acceptors (Eo' = -414 mV), is in equilibrium only at a pH2 of 1 pPa which cannot be maintained by the syntrophic partner bacterium Methanospirillurn hungatei; energy therefore needs to be spent to drive this reaction. Glycolate dehydrogenase activity (0.3-0.96 U . mg protein-') was detected which reduced various artificial electron acceptors such as benzyl viologen, methylene blue, dichloroindophenol, K,[Fe(CN),], and water-soluble quinones.
Fractionation of crude cell extract of the glycolate-fermenting bacterium revealed that glycolate dchydrogcnase, hydrogenase, and proton-translocating ATPase were membrane-bound. Menaquinones wcre found as potential electron camers. Everted membrane vesicles of the glycolate-fermenting bacterium catalyzed ATP-dependent H, formation from glycolate (30-307 nmol H, - min-'.
mg protein-'). Protonophores, inhibitors of proton-translocating ATPase, and the quinone analog antimycin A inhibited H, formation from glycolate, indicating the involvement of proton-motive force to drive the endergonic oxidation of glycolate to glyoxylate with concomitant H, release. This is the first demonstration of a reversed electron transport in syntrophic interspecies hydrogen transfer.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

FRIEDRICH, Michael, Bernhard SCHINK, 1993. Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium. In: FEBS European Journal of Biochemistry. 1993, 217(1), pp. 233-240. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1993.tb18238.x

BibTex

@article{Friedrich1993Hydro-6939,
  year={1993},
  doi={10.1111/j.1432-1033.1993.tb18238.x},
  title={Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium},
  number={1},
  volume={217},
  issn={0014-2956},
  journal={FEBS European Journal of Biochemistry},
  pages={233--240},
  author={Friedrich, Michael and Schink, Bernhard}
}

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/123456789/6939">
    <dcterms:bibliographicCitation>First publ. in: FEBS European Journal of Biochemistry 217 (1993), 1, pp. 233-240</dcterms:bibliographicCitation>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:rights>terms-of-use</dc:rights>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:17Z</dc:date>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6939/1/1993_Friedrich_233_240.pdf"/>
    <dcterms:title>Hydrogen formation from glycolate driven by reversed electron transport in membrane vesicles of a syntrophic glycolate-oxidizing bacterium</dcterms:title>
    <dc:creator>Friedrich, Michael</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:17Z</dcterms:available>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:format>application/pdf</dc:format>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:contributor>Schink, Bernhard</dc:contributor>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dcterms:issued>1993</dcterms:issued>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6939"/>
    <dc:language>eng</dc:language>
    <dc:creator>Schink, Bernhard</dc:creator>
    <dc:contributor>Friedrich, Michael</dc:contributor>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6939/1/1993_Friedrich_233_240.pdf"/>
    <dcterms:abstract xml:lang="eng">Oxidation of glycolate to 2 CO, and 3 H, (AGO' = +36 kJ/mol glycolate) by the proton-reducing, glycolate-fermenting partner bacterium of a syntrophic coculture (strain FlGlyM) depends on a low hydrogen partial pressure (pH). The first reaction, glycolate oxidation to glyoxylate ( E O f = -92 mV) with protons as electron acceptors (Eo' = -414 mV), is in equilibrium only at a pH2 of 1 pPa which cannot be maintained by the syntrophic partner bacterium Methanospirillurn hungatei; energy therefore needs to be spent to drive this reaction. Glycolate dehydrogenase activity (0.3-0.96 U . mg protein-') was detected which reduced various artificial electron acceptors such as benzyl viologen, methylene blue, dichloroindophenol, K,[Fe(CN),], and water-soluble quinones.&lt;br /&gt;Fractionation of crude cell extract of the glycolate-fermenting bacterium revealed that glycolate dchydrogcnase, hydrogenase, and proton-translocating ATPase were membrane-bound. Menaquinones wcre found as potential electron camers. Everted membrane vesicles of the glycolate-fermenting bacterium catalyzed ATP-dependent H, formation from glycolate (30-307 nmol H, - min-'.&lt;br /&gt;mg protein-'). Protonophores, inhibitors of proton-translocating ATPase, and the quinone analog antimycin A inhibited H, formation from glycolate, indicating the involvement of proton-motive force to drive the endergonic oxidation of glycolate to glyoxylate with concomitant H, release. This is the first demonstration of a reversed electron transport in syntrophic interspecies hydrogen transfer.</dcterms:abstract>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Nein