|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4578
|
|
pubmed:dateCreated |
1983-1-7
|
|
pubmed:abstractText |
Low-frequency resonance Raman spectra of transient hemoglobin species were observed within 10 nanoseconds of photolysis. The Raman frequencies of the iron-proximal histidine stretching mode for transient species having either the R or the T quaternary structure are higher than in the corresponding deoxy species. The observed frequency difference in the iron-histidine mode between the R- and T- state transients indicates that there are quaternary structure-dependent protein forces on the iron-histidine bond in the liganded hemoglobins. These differences are interpreted in terms of changes in the tilt of the histidine with respect to the heme plane.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
17
|
|
pubmed:volume |
218
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1244-6
|
|
pubmed:dateRevised |
2007-3-19
|
|
pubmed:meshHeading |
pubmed-meshheading:7146910-Carboxyhemoglobin,
pubmed-meshheading:7146910-Heme,
pubmed-meshheading:7146910-Hemoglobins,
pubmed-meshheading:7146910-Histidine,
pubmed-meshheading:7146910-Humans,
pubmed-meshheading:7146910-Iron,
pubmed-meshheading:7146910-Motion,
pubmed-meshheading:7146910-Myoglobin,
pubmed-meshheading:7146910-Photolysis,
pubmed-meshheading:7146910-Spectrum Analysis, Raman
|
|
pubmed:year |
1982
|
|
pubmed:articleTitle |
Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage.
|
|
pubmed:publicationType |
Journal Article
|
