Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2002-3-18
pubmed:abstractText
Cu(II)-Fe(II) hybrid hemoglobins were investigated by UV-vis, Q-band (35 GHz) EPR and resonance Raman spectroscopies. EPR results indicated that Cu-porphyrin in alpha-subunit within hybrid hemoglobin had either 5- or 4-coordination geometry depending on the pH conditions, while Cu-porphyrin in beta-subunit had only 5-coordination geometry at high and low pH values. These results were consistent with UV-vis absorption results. A new resonance Raman band appeared around 190 cm(-1), which was present whenever 5-coordinated Cu-porphyrin existed in Cu(II)-Fe(II) hybrid hemoglobins irrespective of the coordination number in Fe(II) subunit. This Raman band might be assigned to Cu-N(epsilon) (His) stretching mode. These results are direct demonstration of the existence of coordination changes of Cu-porphyrin in alpha-subunit within hybrid hemoglobin by shifting the molecular conformation from fully unliganded state to intermediately liganded state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
310-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Coordination geometry of Cu-porphyrin in Cu(II)-Fe(II) hybrid hemoglobins studied by Q-band EPR and resonance Raman spectroscopies.
pubmed:affiliation
Division of Biophysical Engineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't