Summary
Hemin 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 reduction of O2 to H2O. However, an independent minor reaction involving a 2-electron transfer with the formation of H2O2 also occurs. These studies on the hemin-catalyzed oxidation of dithiothreitol provide a chemical model for a direct 4-electron reduction of O2 to H2O.
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Abbreviations
- HMGCoA:
-
3-hydroxy-3-methylglutaryl coenzyme A
- DTT:
-
dithiothreitol
- Tris-HCl:
-
tris(hydroxymethyl)-aminomethane hydrochloride
- HEPES:
-
N-2,hydroxylethypiperazine-N′-2-ethane-sulphonic acid
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Usha Devi, S., Ramasarma, T. Hemin-mediated oxidation of dithiothreitol reduces oxygen to H2O. Mol Cell Biochem 77, 111–120 (1987). https://doi.org/10.1007/BF00221919
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DOI: https://doi.org/10.1007/BF00221919