Linked Life Data

6431973

Source:http://linkedlifedata.com/resource/pubmed/id/6431973

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-9-12
pubmed:abstractText
The quenching of coenzyme fluorescence in glycogen phosphorylase b is reinvestigated. Data with anionic quenchers show deviations from the original Stern-Volmer kinetics. A kinetic analysis based on measured lifetime data indicates a collisional quenching process, which is, however, not diffusion-controlled. It is proposed, that the quenching takes place primarily by enzyme-bound quencher species. The observed inhibition of the enzyme reaction by I- and IO-3 is consistent with this hypothesis. The inhibition pattern and spectral investigation refer to a true competition with the substrate, glucose-1-phosphate. So, this dynamic quenching can be regarded as an indicator of rapid conformational fluctuations which bring the two important active-site groups in contact. Effect of ligand binding on the quenching of coenzyme fluorescence should also be revaluated according to these results.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
649-55
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Dynamic interaction between functional groups in the active site of glycogen phosphorylase b.
pubmed:publicationType
Journal Article