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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...
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