Linked Life Data

568006

Source:http://linkedlifedata.com/resource/pubmed/id/568006

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1978-12-20
pubmed:abstractText
The structural basis for intramolecular electron transfer in xanthine oxidase (EC 1.2.3.2) has been probed using temperature-jump perturbation and optical spectroscopic methods. Redox equilibria were found to be temperature-insensitive; hence it is argued that electron transfer is not accompanied by any extensive macromolecular conformational changes. No evidence for absorption phenomena ascribable to optical electron transfer could be found throughout the course of reductive titration of the biological particle. The combined results suggest that long-range electron transfer in the xanthine oxidase can best be described as occurring between only weakly interacting redox sites embedded in a rigid protein matrix.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3061
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
On internal electron transfer in xanthine oxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.