Linked Life Data

1219383

Source:http://linkedlifedata.com/resource/pubmed/id/1219383

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1976-5-25
pubmed:abstractText
The hemoproteins (sperm whale myoglobin, hemoglobin from larvae of Chironomus thummi thummi, bovine hemoglobin) were studied in viscous solvents (saturated sucrose solution, glycerol and water-glycerol solutions) in the temperature range +50 divided by -100 degrees C. At low temperatures the three-phase kinetics of Mb recombination with CO was observed. The velocities of two "fast" reactions did not depend on ligand concentration. This fact indicates that they are due to a so called cage-effect. The formation of the cage is caused apparently by a local change of the solvent state in the heme region. To explain the biphasic "cage" kinetics it has been assumed that during some time after photodissociation myoglobin remains in the "ligand-bound" conformation and reacts with CO faster than the "normal" myoglobin. For other hemoproteins the "cage-effect" was not observed. For all the studied hemoproteins the quantum yield of photodissociation decreased as the temperature decreased. The decrease of quantum yield can be described by the Arrenius law. The rates of the decrease of quantum yield differ for different proteins.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
246-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[The flash-photolysis study of recombination of hemoproteins with carbon monoxide at low temperatures].
pubmed:publicationType
Journal Article, English Abstract