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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1978-3-29
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pubmed:abstractText |
Photodissociation of nitrosyl haemoglobin and nitrosyl hybrids, in which either the alpha or beta subunit is in the nitrosyl form has been stidued at liquid helium temperature (4.2 degrees K) by electron spin resonance and optical absorption spectroscopy. In the presence of inositol hexaphosphate, the photodissociated form of nitrosyl haemoglobin showed an anomalous absorption spectrum in the near infrared region. The experiments with nitrosyl hybrids showed that the alphaNO subunit within the T state haemoglobin is predominantly responsible for the anomalous photodissociated form and the ESR spectrum with three distinct hypefines. The ESR spectrum of alphaNO2betadeoxy2 with inositol hexaphosphate appeared to be very similar to that of the 5-coordinated NO-haem complexes but the absorption spectrum of its photodissociated form was similar to none of protoporphyrin Fe(II) derivatives so far reported. This result suggests that the anomalous photodissociated form may be attributable to some structural distortion of porphyrin or a new electronic state of the haem with different spin state from that of deoxyhaemoglobin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
532
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17-28
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:202327-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:202327-Hemoglobins,
pubmed-meshheading:202327-Humans,
pubmed-meshheading:202327-Macromolecular Substances,
pubmed-meshheading:202327-Nitric Oxide,
pubmed-meshheading:202327-Photolysis,
pubmed-meshheading:202327-Protein Binding,
pubmed-meshheading:202327-Protein Conformation,
pubmed-meshheading:202327-Spectrophotometry, Infrared,
pubmed-meshheading:202327-Temperature
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pubmed:year |
1978
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pubmed:articleTitle |
The effect of quaternary structure on the state of the alpha and beta subunits within nitrosyl haemoglobin. Low temperature photodissociation and the ESR spectra.
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pubmed:publicationType |
Journal Article
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