Cytochrome C is a hydrogen peroxide scavenger in mitochondria.
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.
Wang
Zhi-Bo
ZB
National Laboratory of Biomacromolecule, Center for Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Li
Min
M
Zhao
Yungang
Y
Xu
Jian-Xing
JX
D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D016166:Free Radical Scavengers / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D017665:Hydroxyl Radical / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction; D013384:Succinate Cytochrome c Oxidoreductase / Q000378:metabolism*; D013552:Swine
D003574:Cytochrome c Group; D016166:Free Radical Scavengers; D017665:Hydroxyl Radical; D006861:Hydrogen Peroxide; D013384:Succinate Cytochrome c Oxidoreductase