Purification and Characterization of an NADPH-Cytochrome P450 (Cytochrome c) Reductase from Spearmint (Mentha spicata) Glandular Trichomes

1996 ◽  
Vol 329 (1) ◽  
pp. 9-16 ◽  
Author(s):  
Krishan Ponnamperuma ◽  
Rodney Croteau
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome C ◽  
Glandular Trichomes ◽  
Purification And Characterization ◽  
Mentha Spicata ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome

scholarly journals Purification and characterization of NADPH–cytochrome c reductase from the midgut of the southern armyworm (Spodoptera eridania)

1979 ◽  
Vol 181 (3) ◽  
pp. 593-605 ◽  
Author(s):  
D L Crankshaw ◽  
K Hetnarski ◽  
C F Wilkinson
Keyword(s):  
Cytochrome C ◽  
Active Sites ◽  
Spodoptera Eridania ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Southern Armyworm ◽  
Ping Pong ◽  
Mammalian Liver ◽  
Nadph Cytochrome C Reductase

1. NADPH-cytochrome c reductase was solubilized with bromelain and purified about 400-fold from sucrose/pyrophosphate-washed microsomal fractions from southern armyworm (Spodoptera eridania) larval midguts. 2. The enzyme has a mol.wt. of 70 035 +/- 1300 and contained 2 mol of flavin/mol of enzyme consisting of almost equimolar amounts of FMN and FAD. 3. Aerobic titration of the enzyme with NADPH caused the formation of a stable half-reduced state at 0.5 mol of NADPH/mol of flavin. 4. Kinetic analysis showed that the reduction of cytochrome c proceeded by a Bi Bi Ping Pong mechanism. 5. Apparent Km values for NADPH and cytochrome c and Ki values for NADP+ and 2′-AMP were considerably higher for the insect reductase than for the mammalian liver enzyme. 6. These are discussed in relation to possible differences in the active sites of the enzymes.

The involvement of cytochrome P450 system in the fate of 2,4,6-trinitrotoluene (TNT) in European eel [Anguilla anguilla (Linnaeus, 1758)]

2006 ◽  
Vol 34 (6) ◽  
pp. 1228-1230 ◽  
Author(s):  
C. Della Torre ◽  
I. Corsi ◽  
L. Alcaro ◽  
E. Amato ◽  
S. Focardi
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome C ◽  
Phase Ii ◽  
Reductase Activity ◽  
Anguilla Anguilla ◽  
European Eel ◽  
Cytochrome P450 System ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

TNT (2,4,6-trinitrotoluene) was the most common nitro aromatic explosive available in World War II ammunitions. The presence of ordnance dumped at sea might represent a great concern for marine species living close to dumping sites and the toxicological properties of the chemicals released into the marine environments need to be evaluated. The aim of the present study is to investigate the involvement of CYP (cytochrome P450) system in the metabolism of TNT in marine organisms by using the European eel [Anguilla anguilla (Linnaeus, 1758)] as model species. In vivo exposure to sublethal concentration of TNT (0.5, 1 and 2.5 mg/l) leads to a significant decrease in the phase I CYP1A catalytic activities such as EROD (7-ethoxyresorufin-O-de-ethylase) and MROD (7-methoxyresorufin-O-de-ethylase). On the opposite, a significant increase in NADPH cytochrome c reductase activity as well as phase II UDP-glucuronosyltransferase activity is observed. An inhibition at enzyme level is hypothesized for both CYP1A enzymes, also confirmed by a similar decrease observed after in vitro exposure. An active role of NADPH cytochrome c reductase and phase II enzymes in the TNT metabolism may also be hypothesized.

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