Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin.

@article{Reeder2002CharacteristicsAM,
  title={Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin.},
  author={Brandon J. Reeder and Dimitri A Svistunenko and Martyn A Sharpe and Michael T. Wilson},
  journal={Biochemistry},
  year={2002},
  volume={41 1},
  pages={367-75}
}
At acidic pH values heme-protein cross-linked myoglobin (Mb-H) forms as a product of a peroxide-induced ferric-ferryl redox cycle. There is evidence that this molecule acts as a marker for heme-protein-induced oxidative stress in vivo and may exacerbate the severity of oxidative damage due to its enhanced prooxidant and pseudoperoxidatic activities. Therefore, an understanding of its properties and mechanism of formation may be important in understanding the association between heme-proteins… CONTINUE READING

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