Differential Ability of Cytostatics From Anthraquinone Group to Generate Free Radicals in Three Enzymatic Systems: NADH Dehydrogenase, NADPH Cytochrome P450 Reductase, and Xanthine Oxidase

2003 ◽  
Vol 13 (5) ◽  
pp. 245-252 ◽  
Author(s):  
Jolanta Pawłowska ◽  
Jolanta Tarasiuk ◽  
C. Roland Wolf ◽  
Mark J. I. Paine ◽  
Edward Borowski
Keyword(s):  
Cytochrome P450 ◽  
Free Radicals ◽  
Xanthine Oxidase ◽  
Nadh Dehydrogenase ◽  
Cytochrome P450 Reductase ◽  
Nadph Cytochrome ◽  
P450 Reductase ◽  
Enzymatic Systems ◽  
Nadph Cytochrome P450 Reductase ◽  
Differential Ability

scholarly journals The ability of new formamidine sugar-modified derivatives of daunorubicin to stimulate free radical formation in three enzymatic systems: NADH dehydrogenase, NADPH cytochrome P450 reductase and xanthine oxidase.

2000 ◽  
Vol 47 (1) ◽  
pp. 141-147 ◽  
Author(s):  
J Pawłowska ◽  
J Tarasiuk ◽  
E Borowski ◽  
M Wasowska ◽  
I Oszczapowicz ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Nitrogen Atom ◽  
Xanthine Oxidase ◽  
Nadh Dehydrogenase ◽  
Radical Formation ◽  
Cytochrome P450 Reductase ◽  
Nadph Cytochrome ◽  
P450 Reductase ◽  
Nadph Cytochrome P450 Reductase ◽  
Derivatives Of

Some sterically hindered N-substituted derivatives of daunorubicin are known to be poor substrates for NADH dehydrogenase, NADPH cytochrome P450 reductase and xanthine oxidase. In consequence, poor oxygen radical generation by these compounds is observed. In this study we examined a new family of sugar-N-substituted derivatives of daunorubicin bearing a bulky substituent introduced on the nitrogen atom through the amidine spacer. These compounds were found to be very active in radical formation catalyzed by all three studied enzymes. Thus, the introduction of a heterocyclic ring, even if it is bulky but flexible, on the nitrogen atom of daunosamine moiety through the one-atom spacer (amidine group), does not induce the steric hindrance effect on the interaction of daunorubicin derivatives with these flavoprotein enzymes.

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