Linked Life Data

11540874

Source:http://linkedlifedata.com/resource/pubmed/id/11540874

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-8-28
pubmed:abstractText
Paracoccus halodenitrificans, grown anaerobically in the presence of nitrite, contained membrane and cytoplasmic nitrite reductases. When assayed in the presence of phenazine methosulfate and ascorbate, the membrane-bound enzyme produced nitrous oxide whereas the cytoplasmic enzyme produced nitric oxide. When both enzymes were assayed in the presence of methyl viologen and dithionite, the cytoplasmic enzyme produced ammonia. Following solubilization, the membrane-bound enzyme behaved like the cytoplasmic enzyme, producing nitric oxide in the presence of phenazine methosulfate and ascorbate, and ammonia when assayed in the presence of methyl viologen and dithionite. The cytoplasmic and membrane-bound enzymes were purified to essentially the same specific activity. Only a single nitrite-reductase activity was detected on electrophoretic gels and the electrophoretic behavior of both enzymes suggested they were identical. The spectral properties of both enzymes suggested they were cd-type cytochromes. These data suggest that the products of nitrite reduction by the cd-cytochrome nitrite reductase are determined by the location of the enzyme and the redox potential of the electron donor.
pubmed:keyword
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
S
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0302-8933
pubmed:author
pubmed:issnType
Print
pubmed:volume
145
pubmed:owner
NASA
pubmed:authorsComplete
Y
pubmed:pagination
202-8
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
The purification and properties of a cd-cytochrome nitrite reductase from Paracoccus halodenitrificans.
pubmed:affiliation
Planetary Biology Division, Ames Research Center, Moffett Field, CA 94035, USA.
pubmed:publicationType
Journal Article