Peroxide-dependent oxidations with cytochrome

Peroxide-Dependent Oxidations with Cytochrome P 450. Peroxide-dependent oxidations were carried out exactly as described above except that NADPH-cytochrome P-450 reductase and NADPH were omitted. The peroxide solution (50 fxL of a 20mM solution) was added to the premixed enzyme-substrate solution. The quenching solution was 100 fxL of 30% sodium hydroxide saturated in sodium dithionite. 

The role of these interesting plasma membrane-dependent, vanadate-stimulated NAD(P)H oxidation reactions in cellular metabolism remains to be elucidated, although multiple interactions with cellular metabolism and components are possible including interactions with xanthine oxidase and lipid peroxidation [24], Decavanadate has been shown to enhance cytochrome c reduction [31], and cytochrome c release from mitochondria is associated with initiation of apoptosis. Perhaps the reduced cytochrome c is more readily released from the mitochondria. With increasing emphasis on the redox properties of vanadium being important in its pharmacological effects, it is quite possible that these reactions, either protein dependent or not, may play a role in therapeutic actions of vanadium. 

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