Linked Life Data

8765662

Source:http://linkedlifedata.com/resource/pubmed/id/8765662

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-6
pubmed:abstractText
A new protocol for the preparation of recombinant phytochromes results in significantly higher yields which, for the first time, have made kinetic studies possible. Flash photolysis with nanosecond laser excitation reveals that, in recombinant and native phytochromes, the decay kinetics of the primary photoproducts I700i and the kinetics of the formation of the Pfr form are similar. Phycocyanobilin-containing recombinant phytochrome, however, shows only a monoexponential decay of the I700 intermediate with a time constant of approximately 90 microseconds, and a biexponential formation of the Pfr form, albeit with time constants (approximately 13 and 100 ms) somewhat shorter than those from native phytochrome. Thus the seemingly small structural modification of the chromophore (substitution of the native vinyl for an ethyl group) has a profound influence on the availability of protein conformational rearrangement pathways. The result is therefore of general interest in chromoprotein dynamics.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1011-1344
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
73-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Chromophore-protein interaction controls the complexity of the phytochrome photocycle.
pubmed:affiliation
Max-Planck-Institut für Strahlenchemie, Mülheim an der Ruhr, Germany.
pubmed:publicationType
Journal Article