The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2.
Arch Biochem Biophys
; 484(2): 146-54, 2009 Apr 15.
Article
em En
| MEDLINE
| ID: mdl-19061854
Peroxiredoxin 2 (Prx2) is a 2-Cys peroxiredoxin extremely abundant in the erythrocyte. The peroxidase activity was studied in a steady-state approach yielding an apparent K(M) of 2.4 microM for human thioredoxin and a very low K(M) for H2O2 (0.7 microM). Rate constants for the reaction of peroxidatic cysteine with the peroxide substrate, H2O2 or peroxynitrite, were determined by competition kinetics, k(2) = 1.0 x 10(8) and 1.4 x 10(7) M(-1) s(-1) at 25 degrees C and pH 7.4, respectively. Excess of both oxidants inactivated the enzyme by overoxidation and also tyrosine nitration and dityrosine were observed with peroxynitrite treatment. Prx2 associates into decamers (5 homodimers) and we estimated a dissociation constant K(d) < 10(-23) M(4) which confirms the enzyme exists as a decamer in vivo. Our kinetic results indicate Prx2 is a key antioxidant enzyme for the erythrocyte and reveal red blood cells as active oxidant scrubbers in the bloodstream.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Eritrócitos
/
Peroxirredoxinas
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Uruguai
País de publicação:
Estados Unidos