Linked Life Data

9647763

Source:http://linkedlifedata.com/resource/pubmed/id/9647763

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-7-31
pubmed:abstractText
The complete amino acid sequence of the blue copper-containing nitrite reductase enzyme (NiR) from Achromobacter xylosoxidans has been determined by chemical analysis, supported by high precision mass analysis. The polypeptide chain contains 336 residues with an overall charge of 0, including the +2 state of each of the copper ions. The two NiR enzymes for which the three-dimensional structures have been solved are green in color and have different absorption spectra than those of the blue-colored protein from A. xylosoxidans. The ligands to the two copper atoms are conserved. Therefore, the difference between the blue and the green NiR must depend on subtle changes in the geometry of the type I copper-sulfur bond. Both overall protein charge and active site charge are different in A. xylosoxidans NiR which may reflect the use of azurin as electron donor as opposed to the other enzymes that use pseudoazurin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
247
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
734-40
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
The covalent structure of the blue copper-containing nitrite reductase from Achromobacter xylosoxidans.
pubmed:affiliation
Laboratorium voor Eiwitbiochemie en Eiwitengineering, University of Gent, Belgium.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't