Phosphines as a new structural probe of hemoglobin. 1H-NMR evidence for perturbations in the beta heme pocket induced by a thiol reagent.
Biochim Biophys Acta
; 914(3): 289-93, 1987 Aug 21.
Article
en En
| MEDLINE
| ID: mdl-3620477
ABSTRACT
Binding of trimethylphosphine to myoglobins and hemoglobins from a variety of sources has been examined by 1H-nuclear magnetic resonance. The hemoglobins exhibit two resonances at high field (approx. -3.5 ppm) which have been assigned to PMe3 bound to alpha or to beta subunits. Perturbations in the beta heme pocket induced by a thiol reagent have been detected both in 1H and 31P spectra.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfinas
/
Hemoglobinas
/
Etilmaleimida
/
Hemo
/
Mioglobina
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1987
Tipo del documento:
Article