|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1992-1-14
|
|
pubmed:abstractText |
The allosteric transition in triply ferric hemoglobin has been studied with different ferric ligands. This valency hybrid permits observation of oxygen or CO binding properties to the single ferrous subunit, whereas the liganded state of the other three ferric subunits can be varied. The ferric hemoglobin (Hb) tetramer in the absence of effectors is generally in the high oxygen affinity (R) state; addition of inositol hexaphosphate induces a transition towards the deoxy (T) conformation. The fraction of T-state formed depends on the ferric ligand and is correlated with the spin state of the ferric iron complexes. High-spin ferric ligands such as water or fluoride show the most T-state, whereas low-spin ligands such as cyanide show the least. The oxygen equilibrium data and kinetics of CO recombination indicate that the allosteric equilibrium can be treated in a fashion analogous to the two-state model. The binding of a low-spin ferric ligand induces a change in the allosteric equilibrium towards the R-state by about a factor of 150 (at pH 6.5), similar to that of the ferrous ligands oxygen or CO; however, each high-spin ferric ligand induces a T to R shift by a factor of 40.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-1301061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-1393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-14343300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-210801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2207241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2285779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2306490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2334712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-235946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2548609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2590223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2769761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-2822710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-3365418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-3676434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-4016083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-4363756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-4748831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-4753150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-4761975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-4857061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-5129726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-6088517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-7316964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-909092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1742452-950674
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0006-3495
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
60
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
770-6
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:1742452-Allosteric Regulation,
pubmed-meshheading:1742452-Carboxyhemoglobin,
pubmed-meshheading:1742452-Heme,
pubmed-meshheading:1742452-Hemoglobin A,
pubmed-meshheading:1742452-Hemoglobins,
pubmed-meshheading:1742452-Humans,
pubmed-meshheading:1742452-Iron,
pubmed-meshheading:1742452-Kinetics,
pubmed-meshheading:1742452-Ligands,
pubmed-meshheading:1742452-Mathematics,
pubmed-meshheading:1742452-Methemoglobin,
pubmed-meshheading:1742452-Oxyhemoglobins,
pubmed-meshheading:1742452-Photolysis
|
|
pubmed:year |
1991
|
|
pubmed:articleTitle |
Coupling of ferric iron spin and allosteric equilibrium in hemoglobin.
|
|
pubmed:affiliation |
INSERM U299, Hôpital de Bicêtre, Le Kremlin-Bicêtre, France.
|
|
pubmed:publicationType |
Journal Article
|
