Superoxide from glucose oxidase or from nitroblue tetrazolium?
SI Liochev, I Fridovich - Archives of biochemistry and biophysics, 1995 - Elsevier
SI Liochev, I Fridovich
Archives of biochemistry and biophysics, 1995•ElsevierGlucose oxidase reduces nitroblue tetrazolium, or ferricytochrome c, faster anaerobically
thari aerobically. This result is inconsistent with the conclusion that GO2 can reduce O2 to
O− 2 which is then responsible for the reduction of NET and of cytochrome c. Nevertheless,
the aerobic reductions are partially inhibitable by superoxide dismutase. A scheme of
reactions is proposed which explains why these electron acceptors cause an O− 2
production which does not occur in their absence when O2 is the sole electron acceptor.
thari aerobically. This result is inconsistent with the conclusion that GO2 can reduce O2 to
O− 2 which is then responsible for the reduction of NET and of cytochrome c. Nevertheless,
the aerobic reductions are partially inhibitable by superoxide dismutase. A scheme of
reactions is proposed which explains why these electron acceptors cause an O− 2
production which does not occur in their absence when O2 is the sole electron acceptor.
Glucose oxidase reduces nitroblue tetrazolium, or ferricytochrome c, faster anaerobically thari aerobically. This result is inconsistent with the conclusion that GO2 can reduce O2 to O−2 which is then responsible for the reduction of NET and of cytochrome c. Nevertheless, the aerobic reductions are partially inhibitable by superoxide dismutase. A scheme of reactions is proposed which explains why these electron acceptors cause an O−2 production which does not occur in their absence when O2 is the sole electron acceptor.
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