Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-5-13
pubmed:abstractText
The chemolithoautotrophic archaeon Pyrodictium abyssi isolate TAG 11 gains energy by reducing sulfur with H2 to H2S. From this hyperthermophile, a sulfur-reducing complex catalyzing this reaction was purified 13.5-fold. The native complex exhibited a brownish-yellow colour and showed an apparent molecular mass of 520 kDa. SDS/PAGE revealed the presence of nine different major polypeptides with apparent molecular masses of 82, 72, 65, 50, 47, 42, 40, 30 and 24 kDa. The native complex contained 50-55 mol acid-labile sulfur, 50-55 mol iron, 1.6 mol nickel, 1.2 mol copper, 2.8 mol cytochrome b and 0.3 mol cytochrome c (all per mol native complex). The temperature optimum of the H2:sulfur oxidoreductase complex was 100 degrees C, which is consistent with the physiological growth optimum of the native organism. The complex is extremely heat stable. During 5 h incubation at 100 degrees C, no decrease in H2S-forming activity could be observed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
486-91
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9546664-Amino Acid Sequence, pubmed-meshheading:9546664-Archaea, pubmed-meshheading:9546664-Bacteria, pubmed-meshheading:9546664-Cell Membrane, pubmed-meshheading:9546664-Chromatography, Gel, pubmed-meshheading:9546664-Cytochrome b Group, pubmed-meshheading:9546664-Cytochrome c Group, pubmed-meshheading:9546664-Desulfurococcaceae, pubmed-meshheading:9546664-Hot Temperature, pubmed-meshheading:9546664-Kinetics, pubmed-meshheading:9546664-Macromolecular Substances, pubmed-meshheading:9546664-Molecular Sequence Data, pubmed-meshheading:9546664-Molecular Weight, pubmed-meshheading:9546664-Multienzyme Complexes, pubmed-meshheading:9546664-Oxidation-Reduction, pubmed-meshheading:9546664-Oxidoreductases, pubmed-meshheading:9546664-Sequence Alignment, pubmed-meshheading:9546664-Sequence Homology, Amino Acid, pubmed-meshheading:9546664-Sulfur
pubmed:year
1998
pubmed:articleTitle
Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi.
pubmed:affiliation
Lehrstuhl für Mikrobiologie, Regensburg, Germany. reinhard.dirmeier@biologie.uni-regensburg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't