Linked Life Data

4197931

Source:http://linkedlifedata.com/resource/pubmed/id/4197931

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1973-9-12
pubmed:abstractText
The T(r) and T[unk] states of tyrosinase were treated with NO. EPR spectra of the products observed at 14 degrees K and at 113 degrees K showed mixtures of two signals. One had components in the region of g = 2, about 1200 G wide, and in the region of g = 4, showing hyperfine splitting. The other signal was similar to that arising from isolated Cu(II) ions in an axially symmetric environment. The first signal was indicative of Deltam = 1 and Deltam = 2 transitions arising from magnetic dipole-dipole coupled Cu(II) ion pairs. It closely resembled previously reported EPR spectra obtained from NO-treated hemocyanin, which were confirmed in this study. The normal Curie behavior of the signals between 230 degrees K and 14 degrees K ruled out significant exchange coupling between the ion pairs. The Deltam = 2 signals were not saturable up to 350 mW at 14 degrees K. The broad Deltam = 1 signals could be separated from accompanying signals by the saturation characteristics of the latter at about 10 mW at 14 degrees K. The results establish the presence of a pair of copper ions at the active site of tyrosinase, and a clsoe structural relationship between this active site and that of hemocyanin.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
993-6
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1973
pubmed:articleTitle
Magnetic dipole-dipole coupled Cu(II) pairs in nitric oxide-treated tyrosinase: a structural relationship between the active sites of tyrosinase and hemocyanin.
pubmed:publicationType
Journal Article