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
de 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.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Ribonucleotide reductases
/
Cobamides
/
Lactobacillus leichmannii
Langue:
En
Journal:
Inorg Chem
Année:
2006
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique