Linked Life Data

8805591

Source:http://linkedlifedata.com/resource/pubmed/id/8805591

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1996-11-7
pubmed:databankReference
pubmed:abstractText
Ribonucleotide reductases (RNRs) catalyze the formation of the deoxyribonucleotides that are essential for DNA synthesis. The R2 subunit of Escherichia coli RNR is a homodimer containing one dinuclear iron centre per monomer. A tyrosyl radical is essential for catalysis, and is formed via a reaction in which the reduced, diferrous form of the iron centre activates dioxygen. To help understand the mechanism of oxygen activation, we examined the structure of the diferrous form of R2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1053-64
pubmed:dateRevised
2010-3-24
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site.
pubmed:affiliation
Department of Molecular Biology University of Stockholm S-106 91 Stockholm Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't