Abstract
The ability of succinate cytochrome c reductase (SCR) reduced cytochrome c to scavenge H(2)O(2) was investigated. H(2)O(2), whether added or produced by SCR, was efficiently removed when cytochrome c was reduced by SCR. On the other hand, ferrocytochrome c underwent re-oxidization when H(2)O(2) was added. Thus, these results indicate that cytochrome c reduced by succinate cytochrome c reductase has the ability to regulate H(2)O(max) in mitochondria.
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