Vanadate-stimulated oxidation of NAD(P)H.
Free radical biology & medicine
confidence
Key findings
Vanadate stimulates NAD(P)H oxidation by biological membranes via a free radical chain mechanism; review of mechanism and literature.
View source on PubMed (PMID 2546865) ↗
- Sample size
- Not applicable
- Population
- In vitro biological membranes and NAD(P)H substrates
- Dosing
- Vanadate with NAD(P)H and dihydropyridines
- Duration
- Not applicable
- Route
- In vitro
- Blinding
- not_reported
- Controls
- not_reported
- Drug class
- coenzyme
Full abstract
Vanadate stimulates the oxidation of NAD(P)H by biological membranes because such membranes contain NAD(P)H oxidases which are capable of reducing dioxygen to O2- and because vanadate catalyzes the oxidation of NAD(P)H by O2-, by a free radical chain mechanism. Dihydropyridines, such as reduced nicotinamide mononucleotide (NMNH), which are not substrates for membrane-associated NAD(P)H oxidases, are not oxidized by membranes plus vanadate unless NAD(P)H is present to serve as a source of O2-. When [NMNH] greatly exceeds [NAD(P)H], in such reaction mixtures, one can observe the oxidation of many molecules of NMNH per NAD(P)H consumed. This reflects the chain length of the free radical chain mechanism. We have discussed the mechanism and significance of this process and have tried to clarify the pertinent but confusing literature.