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   <subfield code="a">Identification of intermediate and product from methemoglobin-catalyzed oxidation of o -phenylenediamine in two-phase aqueous—organic system</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[De-Jia Li, Xi-Wen Li, Yu-Xiang Xie, Xiao-Qiang Cai, Guo-Lin Zou]</subfield>
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   <subfield code="a">Methemoglobin (metHb) was used as a mimetic enzyme for peroxidase to catalyze the oxidation reaction of o-phenylenediamine (OPDA) with H2O2 functioning as an oxidant. A reaction intermediate was obtained in two-phase aqueous-organic system and an absorption peak at 710 nm was confirmed to be that of the intermediate in relation to OPDA. The isolated product and intermediate were characterized by UV-V is and IR spectrophotometry and HPLC-tandem mass spectrometry. The results showed that the product is 2,3-diaminophenazine, the molecular mass of the intermediate is 212 daltons, and a conceivable structure of the intermediate is suggested. Combining the catalyzed reaction mechanism of peroxidase and our experimental results, a conceivable oxidation reaction mechanism of OPDA and H2O2 using metHb as catalyst is proposed.</subfield>
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