Linked Life Data

3032675

Source:http://linkedlifedata.com/resource/pubmed/id/3032675

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-6-5
pubmed:abstractText
The ferric spleen green heme-protein exhibits hyperfine-shifted proton resonances between 90 and 20 ppm for the high-spin resting form and the chloride complex, and between 46 and -9.4 ppm for the low-spin nitrite complex. The proton NMR spectral profile of the enzyme is similar to that of lactoperoxidase, but different from those of common heme-proteins. The appearance of a resonance at 76 ppm in the ferrous enzyme shows the presence of a proximal histidine residue linked to the iron. The proton relaxation rates of bulk water indicate that chloride binds to the sixth position of the iron in the chloride complex of the enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
214
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Proton magnetic resonance of the bovine spleen green heme-protein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.