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Citation: Li Zhen, Xia Chun-Gu, Wei Chi-Li, Li Shu-Ben. Rapid-Mixing Stopped-Flow Spectra of Manganese(Pentafluorophenyl) Porphyrin Enzyme-Mimic Systems[J]. Acta Physico-Chimica Sinica, ;1999, 15(08): 715-719. doi: 10.3866/PKU.WHXB19990810 shu

Rapid-Mixing Stopped-Flow Spectra of Manganese(Pentafluorophenyl) Porphyrin Enzyme-Mimic Systems

1.
State Key Laboratory for Oxo Synthesis Selective Oxidation,Lanzhou Institute of Chemical Physics,Chinese Academy of Science,Lanzhou 730000

Received Date: 5 October 1998
Available Online: 15 August 1999

The reactions of manganese (pentafluorophenyl) porphrin complex, MnⅢ(TFPP ) C1 with two oxidants iodosobenzene (PhIO) and m-chloroperoxybenzoic acid(m-CPBA) under ambient conditions have been investigated by stopped-flow spectraphotometry. It is shown that high-valent oxomanganese porphyrin complexes and dimeric μ-oxo manganese(IV) porphrin complex intermediates were produced in the reaction between MuⅢ (TFPP)C1 and PhIO, and the oxomanganese porphrin complexes almost completely decomposed to the corresponding MnⅢ（TFPP)C1 species. With m-CPBA as the oxygen donor, only a few short-lived high-valent oxomanganese porpdrin complexes were produced. Epoxidization of 1, 4 - diphenylbutadiene (DPBD) by MnⅢ(TFPP ) C1 with PhIO and m-CPBA showed that since a stable species was produced in the reaction of MuⅢ (TFPP)C1 with m-CPBA, so the reactivity of this model system was lower than that with oxidant PhIO.
- stopped-flow,
- Manganese porphrin complexes,
- Iodosobenzene,
- m-chloroperoxybenzoin cid,
- Epoxidization
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