• Applied Chemistry for Engineering
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• v.17 no.5
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• pp.552-556
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• 2006

An advanced oxidation process catalyzed by iron ions in the presence of hydrogen peroxide, the so-called Fenton's reaction, has been applied to the treatment of steam generator chemical cleaning waste containing highly concentrated iron(III)- ethyl-enediaminetetraaceticacid (Fe(III)-EDTA) of 70000 mg/L. The experiments for the degradation of Fe(III)-EDTA were carried out not only with a simulated waste, but also with the real one. The effect of pH and the amount of hydrogen peroxide added to the waste on the degradation was examined, and the results were discussed in several aspects. The optimal pH to maximize the degradation efficiency was dependent on the amount of hydrogen peroxide added to the waste. i.e., when the amount of hydrogen peroxide was different, maximum degradation efficiency was obtained at different pH's. The optimal amount of hydrogen peroxide relative to that of Fe(III)-EDTA was found to be 24.7 mol ($H_{2}O_{2}$)/mol (Fe(III)-EDTA) at pH around 9.

• Biomedical Science Letters
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• v.4 no.1
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• pp.1-9
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• 1998

A Corynebacterium diphtheriae iron-repressible gene dirA, that was homologous to TSA of Saccharomyces cerevisiae and AhpC subunit of Salmonella typhimurium alkyl hydroperoxide reductase, was amplified with PCR and expressed in E. coli. The DirA purified from the transformed E. coli crude extracts prevented the inactivation of enzyme caused by metal-catalyzed oxidation (MCO) system containing thiols but not by ascorbate/Fe$^{3+}$/$O_2$ MCO system. The DirA concentration, which inhibited the inactivation of glutamine synthetase by 50% (IC$_{50}$) against MCO system, was 0.12 mg/ml. The multimeric forms of DirA were converted to the monomeric form in SDS-PAGE under the thioredoxin system comprised of NADPH, Saccharomyces cerevisiae thioredoxin reductase, and thioredoxin. Also, DirA showed thioredoxin dependent peroxidase activity. All of these results were consistent with the characteristics of a thiol specific antioxidant (TSA) protein having two conserved cysteine residues.