Linked Life Data

9326366

Source:http://linkedlifedata.com/resource/pubmed/id/9326366

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-11-6
pubmed:abstractText
The hydration properties of the oxidized form of horse heart cytochrome c have been studied by 1H NMR spectroscopy. Application of ePHOGSY (enhanced protein hydration observed through gradient spectroscopy) experiments over a paramagnetic molecule provided firm spectroscopic evidence of the presence of a water molecule in the heme crevice. A few intermolecular NOEs have been used to locate the water molecule at about 0.65 nm away from the iron atom and to compare the position observed in solution with that observed in the crystal structure and in solution for the reduced state. The resulting picture is that there is a detectable movement of the water molecule upon oxidation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
415
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
ePHOGSY experiments on a paramagnetic protein: location of the catalytic water molecule in the heme crevice of the oxidized form of horse heart cytochrome c.
pubmed:affiliation
Department of Chemistry, University of Florence, Italy. bertini@risc1.lrm.fi.cnr.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't