Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1982-7-19
|
| pubmed:abstractText |
Low-temperature photodissociation of oxygen from oxy-cobalt myoglobin was studied by single-crystal electron paramagnetic resonance (EPR) spectroscopy at 5 K. The photolyzed oxy-cobalt myoglobin exhibited an EPR spectrum consisting of two nonequivalent sets (species I and II) of the principal values and eigenvectors of the g tensors: g1I = 3.55, g2I = 3.47, and g3I = 2.26 for species I, and g1II = 2.04, g2II = 1.93, and g3II = 1.86 for species II, which resembled neither the deoxy nor the oxy form. Possible models of the photodissociated state of oxy-cobalt myoglobin are proposed by comparison with cobalt porphyrin complexes. The photolyzed product of nitric oxide-cobalt myoglobin exhibited new EPR signals at g = 4.3 and a very broad signal at around g = 2. The principal g values have been determined from the single-crystal EPR measurements: g1 = 4.39, g2 = 4.27, and g3 = 4.00. Analysis of another EPR signal around g = 2 was difficult due to its broadness. Magnetic interactions were observed. An isotropic EPR signal at g = 4.3 suggested a weakly spin-coupled system between cobaltous spin (S = 1/2 or 3/2) and nitric oxide spin (S = 1/2).
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
16
|
| pubmed:volume |
21
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1431-7
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1982
|
| pubmed:articleTitle |
Single-crystal electron paramagnetic resonance studies of photolyzed oxy- and nitric oxide-cobalt myoglobins.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|