Reaction of the Hansenula anomala flavocytochrome b2 and cytochrome b2 core with inorganic outer sphere redox compounds.
Biochimie
; 77(7-8): 531-8, 1995.
Article
em En
| MEDLINE
| ID: mdl-8589064
The oxidation of reduced cytochrome b2 core and flavocytochrome b2 by three inorganic outer sphere compounds, Fe(CN)6(3-), Co(phen)3(3+) and Mn(CyDTA) (H2O)-, has been studied by stopped-flow. The reaction with Fe(CN)6(3-) is very rapid; the second order rate constants at 10 degrees C (pH 7) and I = 0.02 M are k = 1 x 10(8) M-1 s-1 and 1 x 10(7) M-1 s-1 for cytochrome b2 core and flavocytochrome b2, respectively. The reaction between cytochrome b2 core and Co(phen)3(3+), too fast at pH 7.0, has been characterized at 10 degrees C and pH 4.0; the second order rate constant is k = 2 x 10(7) M-1 s-1 and becomes 4 x 10(8) M-1 s-1 at pH 6.5. The reaction between flavocytochrome b2 and Co(phen)3(3+) has a second order rate constant k = 2 x 10(7) M-1 s-1 at pH 7.0, 10 degrees C. The oxidation of both proteins by Mn(CyDTA)(H2O)- is characterized by a second order rate constant k = 2.8 x 10(6) M-1 s-1 and 2.3 x 10(5) M-1 s-1 for cytochrome b2 core and flavocytochrome b2, respectively, at pH 7.0 and 10 degrees C. The reactivity of the b2 heme towards the outer sphere oxidants is higher than that reported for heme c in bacterial and eukaryotic cytochrome c. The larger delta E and the larger accessibility of the b2 heme can account for this result. The flavodehydrogenase domain seems to modulate the electron transfer also to these inorganic compounds, as found previously in the case of macromolecular electron acceptors.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pichia
/
Proteínas Fúngicas
/
Transporte de Elétrons
/
Heme
/
L-Lactato Desidrogenase
Idioma:
En
Revista:
Biochimie
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Itália