Acta Phys. -Chim. Sin. ›› 1999, Vol. 15 ›› Issue (08): 715-719.doi: 10.3866/PKU.WHXB19990810

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

Li Zhen, Xia Chun-Gu, Wei Chi-Li, Li Shu-Ben   

  1. State Key Laboratory for Oxo Synthesis Selective Oxidation,Lanzhou Institute of Chemical Physics,Chinese Academy of Science,Lanzhou 730000
  • Received:1998-10-05 Revised:1999-02-02 Published:1999-08-15
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Abstract:

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.

Key words: stopped-flow, Manganese porphrin complexes, Iodosobenzene, m-chloroperoxybenzoin cid, Epoxidization