scholarly journals Adrenodoxin reductase.adrenodoxin complex. Flavin to iron-sulfur electron transfer as the rate-limiting step in the NADPH-cytochrome c reductase reaction.

1979 ◽  
Vol 254 (8) ◽  
pp. 2766-2774
Author(s):  
J.D. Lambeth ◽  
H. Kamin
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Rate Limiting Step ◽  
Iron Sulfur ◽  
Limiting Step ◽  
Rate Limiting ◽  
Nadph Cytochrome C Reductase

A chimeric iron-sulfur flavoprotein endowed with NADPH-cytochrome c reductase activity

1996 ◽  
Vol 24 (1) ◽  
pp. 22S-22S ◽  
Author(s):  
Giuliana Zanetti ◽  
Luciano Piubelli ◽  
Roberta Zucca Tanci ◽  
Alessandro Aliverti
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Iron Sulfur ◽  
Nadph Cytochrome C Reductase

Is the Internal Electron Transfer the Rate-Limiting Step in the Catalytic Cycle of Cytochrome c Oxidase?

1988 ◽  
Vol 550 (1 Cytochrome Ox) ◽  
pp. 161-166 ◽  
Author(s):  
PAOLO SARTI ◽  
GIOVANNI ANTONINI ◽  
RANCESCO MALATESTA ◽  
BEATRICE VALLONE ◽  
MAURIZIO BRUNORI
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Catalytic Cycle ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Internal Electron ◽  
Rate Limiting

scholarly journals Étude de l’effet du cadmium et du benzo[a]pyrène sur des enzymes de phase I et phase II de biotransformation chez le polychète Nereisdiversicolor

2009 ◽  
Vol 22 (3) ◽  
pp. 451-459
Author(s):  
Zied Bouraoui ◽  
Jihene Ghedira ◽  
Jamel Jebali ◽  
Mohamed Banni ◽  
Cristelle Clerendeau ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Phase I ◽  
Phase Ii ◽  
Nereis Diversicolor ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

Résumé Le présent travail reporte l’effet du cadmium (Cd), du benzo[a]pyrène (B[a]P) ainsi que leur mélange (Cd/B[a]P), à 1 µM, sur les activités d’enzymes impliqués dans la phase I et la phase II de biotransformation chez le polychète Nereis diversicolor en fonction du temps (après 12, 24, 36 et 48 h). L’effet d’une contamination aiguë par du cadmium à une dose de 1 µM après 12, 24 et 36 h montre une inhibition de l’activité NADPH cytochrome C réductase chez les individus contaminés comparés à leurs témoins relatifs, alors que le seul effet du cadmium sur l’activité glutathion-S-transférase n’est enregistré qu’après 36 h d’exposition. Quant au benzo[a]pyrène, les résultats montrent une augmentation significative de l’activité NADPH cytochrome C réductase après 12, 24 et 36 h d’exposition, alors que pour l’activité glutathion-S‑transférase, la variation significative entre les animaux témoins et traités n’est enregistrée qu’à 36 h d’exposition. Le mélange (Cd/B[a]P) inhibe l’activité NADPH cytochrome C réductase chez les individus traités par comparaison aux témoins relatifs et montre un effet inducteur sur l’activité GST sauf après 36 h d’exposition. Ces résultats montrent ainsi les interactions entre les polluants ainsi que leurs effets sur les organismes.

Intracellular distribution of NADPH-cytochrome c reductase in rat hepatocytes studied by direct ferritin-immunoelectron microscopy

1981 ◽  
Vol 50 (1) ◽  
pp. 181-198
Author(s):  
K. Aoi ◽  
Y. Fujii-Kuriyama ◽  
Y. Tashiro
Keyword(s):  
Cytochrome C ◽  
Immunoelectron Microscopy ◽  
Plasma Membranes ◽  
Control Level ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Cross Sectional ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

NADPH-cytochrome c reductase was purified from rat liver microsomes and the monospecific antibodies to the reductase were prepared from the antiserum by affinity chromatography using immunoadsorbent gel. Ferritin was coupled to the specific antibodies and the approximately equimolar conjugates were isolated by gel filtration. By direct ferritin-immunoelectron microscopy, using these conjugates, it was revealed that the ferritin particles are localized exclusively on the microsomal vesicles and the outer nuclear envelope. In contrast, binding of ferritin particles to Golgi membranes, outer mitochondrial membranes and plasma membranes was slight and at control level. On each microsomal vesicle, the ferritin particles were distributed heterogeneously, sometimes forming clusters. An assay of the binding of equimolar conjugates with microsomes showed that microsomes bind approximately 1 mol of antibody per mol of reductase. From these data the maximum number of ferritin particles that can bind with microsomes was calculated. This number is in agreement with the average number of ferritin particles bound per microsome, as determined experimentally by observing a number of cross-sectional profiles of microsomal vesicles previously incubated with the conjugates at saturation level. This showed that the distribution of the reductase could be analysed semi-quantitatively by the present ferritin-immunoelectron-microscopical analyses. It was also shown that smooth microsomes can bind more conjugates than rough microsomes. The average number of ferritin particles on each microsomal vesicle increased in proportion to the increase in the amount of reductase in the microsomes after treatment with phenobarbital. Finally, the non-random distribution of ferritin particles on microsomal vesicles was confirmed by statistical analysis of electron micrographs of a number of the labelled microsomes.

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