|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1981-8-20
|
|
pubmed:abstractText |
The dioxygen--iron bond in oxyhemerythrin is shown to be photosensitive. The recombination reaction after photodissociation depends strongly on solvent viscosity. In water (eta = 1 centipoise or 1 x 10(-3) Pa . s) the recombination is monophasic and second-order in solvent oxygen concentration, with a bimolecular rate coefficient of 2.9 x 10(7) M-1 s-1. In a glycerol/water mixture (eta = 180 centipoise) a concentration-dependent geminate recombination process is also seen. This opens a class of proteins to study by flash photolysis.
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
78
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2307-9
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1981
|
|
pubmed:articleTitle |
Hemerythrin's oxygen-binding reaction studied by laser photolysis.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
