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.
MeSH terms
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Animals
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Cytochrome c Group / metabolism*
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Electron Spin Resonance Spectroscopy
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Electron Transport
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Free Radical Scavengers / metabolism*
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Hydrogen Peroxide / metabolism*
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Hydroxyl Radical / metabolism*
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Mitochondria, Heart / enzymology*
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Oxidation-Reduction
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Succinate Cytochrome c Oxidoreductase / metabolism*
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Swine
Substances
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Cytochrome c Group
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Free Radical Scavengers
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Hydroxyl Radical
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Hydrogen Peroxide
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Succinate Cytochrome c Oxidoreductase