THE PH-DEPENDENCE OF THE MECHANISM OF REACTION OF HYDROGEN-PEROXIDE WITH A NONAGGREGATING, NON-MU-OXO DIMER-FORMING IRON(III) PORPHYRIN IN WATER
THE PH-DEPENDENCE OF THE MECHANISM OF REACTION OF HYDROGEN-PEROXIDE WITH A NONAGGREGATING, NON-MU-OXO DIMER-FORMING IRON(III) PORPHYRIN IN WATER
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DOI：
10.1073/pnas.83.13.4646
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发表时间：
1986-07-01
影响因子：
11.1
通讯作者：
LEE, WA
中科院分区：
文献类型：
--
作者：
BRUICE, TC;ZIPPLIES, MF;LEE, WA
The reaction of hydrogen peroxide with 5,10,15,20-tetrakis(2,6-dimethyl-3-sulfonatophenyl)porphinatoiron(III) hydrate [(P)FeIII(H2O)] has been investigated in water between pH 1 and pH 12. The water-soluble (P)FeIII(H2O) neither aggregates nor forms a .mu.-oxo dimer. The pH dpeendence and rate-limiting second-order rate constants (kly) for oxygen trnsfer from H2O2 and HO2- to the iron(III) porphyrin were determined by trapping of the resultant higher-valent iron-oxo porphyrin species with 2,2''-azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS). Reactions were monitored spectrophometrically by following the appearance of the radical ABTS.cntdot.+. From a plot of the logarithm of the determine second-order rate constants for reaction of hydrogen peroxide with iron(III) porphyrin vs. pH, the composition of the transition states can be assigned for the three reactions that result in oxyen transfer to yield a higher-valent iron-ovo porphyrin species. The latter not only reacts with ABTS to provide ABTS.cntdot.+ in a peroxidase-type reaction but also reacts with hydrogen peroxide to provide O2 in a catalase-type reaction. The nitrogen base 2,4,6-collidine serves as a catalyst for oxygen transfer from hydrogen peroxide to the (P)FeIII(H2O) and (P)FeIII(HO) species. The preferred mechanism involves a 1,2-proton shift concered with heterolytic cleavage of the peroxide O.sbd.O bond. An analogous mechanism is believed to occur in the peroxidase enzymes.
