Hemin-mediated oxidation of dithiothreitol reduces oxygen to H2O

@article{UshaDevi2004HeminmediatedOO,
  title={Hemin-mediated oxidation of dithiothreitol reduces oxygen to H2O},
  author={S. Usha Devi and Tangirala Ramasarma},
  journal={Molecular and Cellular Biochemistry},
  year={2004},
  volume={77},
  pages={111-120}
}
SummaryHemin catalyses the oxidation of dithiothreitol. One mole of oxygen is consumed for every 2 moles of dithiothreitol oxidized and the product is shown by spectral studies to be the intramolecular disulphide. The reaction shows a specificity for dithiol and for free heme moieties. Hemin molecules exhibit cooperativity in oxygen reduction. Oxygen radicals do not seem to be involved. H2O2 is not required for this oxidation of dithiothreitol and does not appear to be an intermediate in the… 

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References

SHOWING 1-10 OF 10 REFERENCES
Hemin-mediated oxidative degradation of proteins.
The Catalytic Action of Traces of Iron on the Oxidation of Cysteine and Glutathione.
TLDR
The theory that the so-called autoxidation of cysteine is in reality a catalysis by iron is put forward, and cystine can be reduced by an aqueous solution of potassium cyanide, and Abderhalden and Wertheimer confirmed this, finding that cyStine is reduced by diluteassium cyanide solution, the reduction.
Analysis and computer simulation of aerobic oxidation of reduced nicotinamide adenine dinucleotide catalyzed by horseradish peroxidase.
TLDR
Time courses of NADH oxidation, O2 consumption, H2O2 accumulation, and formation of enzyme intermediates could be simulated with an electronic computer using 11 elementary reactions and 9 rate equations to discuss the mechanism for oscillatory responses of the reaction.
The effects of chemical porphyrogens and drugs on the activity of rat liver tryptophan pyrrolase.
TLDR
It is suggested that the saturation of rat liver apo-(tryptophan pyrrolase) with its haem activator can be modified by treatment known to cause destruction, inhibition of synthesis, increased utilization and enhanced synthesis of liver haem.
Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation.
  • D. Ziegler
  • Biology, Computer Science
    Annual review of biochemistry
  • 1985
PERSPECTIVES AND SUMMARY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 306 REGULATION BY THIOL : DISULFIDE EXCHANGE-AN
Address for offprints." T. Ramasarma, Department of Biochemistry, Indian Institute
  • Ann Rev Biochem 54:305-329,
  • 1985
Biochemistry 16 : 1913 - 1920 , 1977 5
  • 1984