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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1981-8-20
|
| pubmed:abstractText |
A copper-containing nitrite reductase was purified and crystallized from a potent denitrifying bacterium, Alcaligenes faecalis strain S-6. The enzyme was composed of 4 subunits with a molecular weight of about 30,000, each containing 1 atom of Cu2+. Nitric oxide was identified as a main reduction product from nitrite in the enzyme-catalyzed reaction. The enzyme activity was inhibited strongly by KCN but only slightly by sulfhydryl reagents such as p-chloromercuribenzoate and N-ethylmaleimide.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-924X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
89
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
453-61
|
| pubmed:dateRevised |
2007-12-19
|
| pubmed:meshHeading |
pubmed-meshheading:7240122-Alcaligenes,
pubmed-meshheading:7240122-Copper,
pubmed-meshheading:7240122-Crystallography,
pubmed-meshheading:7240122-Hydrogen-Ion Concentration,
pubmed-meshheading:7240122-Isoelectric Point,
pubmed-meshheading:7240122-Kinetics,
pubmed-meshheading:7240122-Molecular Weight,
pubmed-meshheading:7240122-NADH, NADPH Oxidoreductases,
pubmed-meshheading:7240122-Nitrite Reductases,
pubmed-meshheading:7240122-Spectrum Analysis
|
| pubmed:year |
1981
|
| pubmed:articleTitle |
Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6.
|
| pubmed:publicationType |
Journal Article
|