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- W2619132258 abstract "MauG is a diheme enzyme that utilizes two covalently bound c-type heme centers. We report here step-wise oxidations of a synthetic analogue of MauG in which two heme centers are bridged covalently through a flexible linker containing a pyrrole moiety. One- and two-electron oxidations produce monocation radical and dication diradical intermediates, respectively, which, being highly reactive, undergo spontaneous intramolecular rearrangement involving the pyrrole bridge itself to form indolizinium-fused chlorin-porphyrin and spiro-porphyrinato heterodimers. Unlike in MauG, where the two oxidizing equivalents produce the bis-FeIV redox state, the synthetic analogue of the same, however, stabilizes two ferric hemes, each coupled with a porphyrin π-cation radical. The present study highlights the possible role played by the bridge in the electronic communication." @default.
- W2619132258 created "2017-06-05" @default.
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- W2619132258 date "2017-07-07" @default.
- W2619132258 modified "2023-10-16" @default.
- W2619132258 title "Probing Bis‐Fe<sup>IV</sup>MauG: Isolation of Highly Reactive Radical Intermediates" @default.
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- W2619132258 doi "https://doi.org/10.1002/chem.201702321" @default.
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