Linked Life Data

19109051

Source:http://linkedlifedata.com/resource/pubmed/id/19109051

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-1-26
pubmed:abstractText
Because of catalysis of horseradish peroxidase, the tyrosine reacted with H(2)O(2) to form the product S which was a strong fluorescence substance. To the product S, the quercetin was acted as a quencher. The fluorescence quenching mechanism was studied by the measurement of fluorescence lifetime and based on the Stern-Volmer plot. The reaction mechanism, which was the static quenching process between quercetin and product S, was studied. The binding constant, K=4.03 x 10(5) L mol(-1) and the number of binding sites n=1.09, were obtained against this reaction. The thermodynamic parameters were estimated. The data, DeltaH=-75.68 kJ mol(-1), DeltaS=-147.9JK(-1) mol(-1) and DeltaG=-29.17 kJ mol(-1) showed that the reaction was spontaneous and exothermic. What is more, both DeltaH and DeltaS were negative values indicated that van der Waals interaction and hydrogen bonding were the predominant intermolecular forces between quercetin and product S.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1386-1425
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
572-6
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Study of fluorescence quenching mechanism between quercetin and tyrosine-H(2)O(2)-enzyme catalyzed product.
pubmed:affiliation
College of Chemistry, Chemical Engineering and Materials Science, Shandong Normal University, Jinan 250014, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't