NMR observations of 13C-enriched coenzyme B12 bound to the ribonucleotide reductase from Lactobacillus leichmannii.
Inorg Chem
; 45(23): 9172-4, 2006 Nov 13.
Article
en En
| MEDLINE
| ID: mdl-17083212
ABSTRACT
The 13C NMR resonance and one-bond 1H-13C coupling constants of coenzyme B12 enriched in 13C in the cobalt-bound carbon have been observed in the complex of the coenzyme with the B12-dependent ribonucleotide reductase from Lactobacillus leichmannii. Neither the 13C NMR chemical shift nor the 1H-13C coupling constants are significantly altered by binding of the coenzyme to the enzyme. The results suggest that ground-state Co-C bond distortion is not utilized by this enzyme to activate coenzyme B12 for C-Co bond homolysis.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ribonucleótido Reductasas
/
Cobamidas
/
Lactobacillus leichmannii
Idioma:
En
Revista:
Inorg Chem
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos