Hydrogen metabolism in aerobic hydrogen-oxidizing bacteria

Loading...
Thumbnail Image
Date
1978
Authors
Schlegel, Hans G.
Editors
Contact
Journal ISSN
Electronic ISSN
ISBN
Bibliographical data
Publisher
Series
DOI (citable link)
ArXiv-ID
International patent number
Link to the license
EU project number
Project
Open Access publication
Collections
Restricted until
Title in another language
Research Projects
Organizational Units
Journal Issue
Publication type
Journal article
Publication status
Published in
Biochimie ; 60 (1978). - pp. 297-305. - ISSN 0300-9084
Abstract
A survey on organisms able to use molecular hydroqen as electron donor in the enerqy-yielding process is presented. In the group of the aerobic hydrogen-oxidizing bacteria so far two types of hydrogenases have been en- countered, a NAD-reducing, soluble enzyme (H2 : NAD oxidoreductase) and a membrane-bound enzyme unable to reduce pyridine nucleotides. With respect to the distribution of both types of hydrogenases three groups of hydroqen-oxidizing bacteria can be diffentiated containing (i) both types (Alcaligenes eutrophus), (ii) a soluble enzyme only (Nocardia opaca lb), and (iii) a membrane-bound hydrogenase only (majority of genera and species). The results of studies on the NAD-specific hydrogenase of A. eutrophus are summarized. Results on the solubilization and purification of the membrane-bound hydrogenase of A. eutrophus are presented in detail. The enzyme was solubilized from purified membranes by Triton X-100 and sodium desoxycholate or phospholipase D. The crude membrane extract was fractionated by ammonium sulfate precipitation and chromatography on carboxymethylcellulose at pH 5.5. The enzyme was stable in potassium phosphate buffer ; it resembles the soluble enzyme with respect to stability under oxidizinq conditions. Further biochemical and immunological data indicate, however, that both enzymes are different with respect to their native structure.
Summary in another language
Subject (DDC)
570 Biosciences, Biology
Keywords
Conference
Review
undefined / . - undefined, undefined. - (undefined; undefined)
Cite This
ISO 690SCHINK, Bernhard, Hans G. SCHLEGEL, 1978. Hydrogen metabolism in aerobic hydrogen-oxidizing bacteria. In: Biochimie. 60, pp. 297-305. ISSN 0300-9084
BibTex
@article{Schink1978Hydro-6669,
  year={1978},
  title={Hydrogen metabolism in aerobic hydrogen-oxidizing bacteria},
  volume={60},
  issn={0300-9084},
  journal={Biochimie},
  pages={297--305},
  author={Schink, Bernhard and Schlegel, Hans G.}
}
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/123456789/6669">
    <dc:contributor>Schlegel, Hans G.</dc:contributor>
    <dcterms:issued>1978</dcterms:issued>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6669/1/Hydrogen_metabolism_in_aerobic_hydrogen_oxidizing_bacteria.pdf"/>
    <dc:rights>terms-of-use</dc:rights>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:title>Hydrogen metabolism in aerobic hydrogen-oxidizing bacteria</dcterms:title>
    <dc:contributor>Schink, Bernhard</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6669"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6669/1/Hydrogen_metabolism_in_aerobic_hydrogen_oxidizing_bacteria.pdf"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:28:13Z</dc:date>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Schink, Bernhard</dc:creator>
    <dc:language>eng</dc:language>
    <dcterms:bibliographicCitation>First publ. in: Biochimie 60 (1978), pp. 297-305</dcterms:bibliographicCitation>
    <dc:creator>Schlegel, Hans G.</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:28:13Z</dcterms:available>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:abstract xml:lang="eng">A survey on organisms able to use molecular hydroqen as electron donor in the enerqy-yielding process is presented. In the group of the aerobic hydrogen-oxidizing bacteria so far two types of hydrogenases have been en- countered, a NAD-reducing, soluble enzyme (H2 : NAD oxidoreductase) and a membrane-bound enzyme unable to reduce pyridine nucleotides. With respect to the distribution of both types of hydrogenases three groups of hydroqen-oxidizing bacteria can be diffentiated containing (i) both types (Alcaligenes eutrophus), (ii) a soluble enzyme only (Nocardia opaca lb), and (iii) a membrane-bound hydrogenase only (majority of genera and species). The results of studies on the NAD-specific hydrogenase of A. eutrophus are summarized. Results on the solubilization and purification of the membrane-bound hydrogenase of A. eutrophus are presented in detail. The enzyme was solubilized from purified membranes by Triton X-100 and sodium desoxycholate or phospholipase D. The crude membrane extract was fractionated by ammonium sulfate precipitation and chromatography on carboxymethylcellulose at pH 5.5. The enzyme was stable in potassium phosphate buffer ; it resembles the soluble enzyme with respect to stability under oxidizinq conditions. Further biochemical and immunological data indicate, however, that both enzymes are different with respect to their native structure.</dcterms:abstract>
    <dc:format>application/pdf</dc:format>
  </rdf:Description>
</rdf:RDF>
Internal note
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Contact
URL of original publication
Test date of URL
Examination date of dissertation
Method of financing
Comment on publication
Alliance license
Corresponding Authors der Uni Konstanz vorhanden
International Co-Authors
Bibliography of Konstanz
No
Refereed