Low temperature photodissociation studies of ferrous hemoglobin and myoglobin complexes by Mössbauer spectroscopy.
Biochim Biophys Acta
; 428(2): 281-90, 1976 Apr 23.
Article
em En
| MEDLINE
| ID: mdl-1276159
ABSTRACT
57Fe-enriched complexes of hemoglobin and myoglobin with CO and O2 were photodissociated at 4.2 degrees K, and the resulting spectra were compared with those of the deoxy forms. Differences in both quadrupole splitting and isomer shift were noted for each protein, the photoproducts having smaller isomer shift and larger quadrupole splitting than the deoxy forms. The photoproducts of HbCO and HbO2 had narrow absorption lines, indicating a well-defined iron environment. The corresponding myoglobin species had broader absorption lines, as did both deoxy forms. The weak absorption lines of photodissociated NO complexes appeared to be wide, possibly indicating magnetic interaction with the unpaired electron of the nearby NO.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hemoglobinas
/
Compostos Ferrosos
/
Ferro
/
Mioglobina
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
1976
Tipo de documento:
Article