Structural determinants for the formation of sulfhemeprotein complexes.
Biochem Biophys Res Commun
; 400(4): 489-92, 2010 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-20732304
ABSTRACT
Several hemoglobins were explored by UV-Vis and resonance Raman spectroscopy to define sulfheme complex formation. Evaluation of these proteins upon the reaction with H(2)O(2) or O(2) in the presence of H(2)S suggest (a) the formation of the sulfheme derivate requires a HisE7 residue in the heme distal site with an adequate orientation to form an active ternary complex; (b) that the ternary complex intermediate involves the HisE7, the peroxo or ferryl species, and the H(2)S molecule. This moiety precedes and triggers the sulfheme formation.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Oxígeno
/
Sulfahemoglobina
/
Agua
/
Histidina
/
Sulfuro de Hidrógeno
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2010
Tipo del documento:
Article
País de afiliación:
Puerto Rico