Activation of a Non-Heme FeIII -OOH by a Second FeIII to Hydroxylate Strong C-H Bonds: Possible Implications for Soluble Methane Monooxygenase.
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SUBMITTER: Kal S
PROVIDER: S-EPMC6555659 | biostudies-literature | 2019 Jun
REPOSITORIES: biostudies-literature
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Activation of a Non-Heme Fe<sup>III</sup> -OOH by a Second Fe<sup>III</sup> to Hydroxylate Strong C-H Bonds: Possible Implications for Soluble Methane Monooxygenase.
Kal Subhasree S Que Lawrence L
Angewandte Chemie (International ed. in English) 20190509 25
Non-heme iron oxygenases contain either monoiron or diiron active sites, and the role of the second iron in the latter enzymes is a topic of particular interest, especially for soluble methane monooxygenase (sMMO). Herein we report the activation of a non-heme Fe<sup>III</sup> -OOH intermediate in a synthetic monoiron system using Fe<sup>III</sup> (OTf)<sub>3</sub> to form a high-valent oxidant capable of effecting cyclohexane and benzene hydroxylation within seconds at -40 °C. Our results show ...[more]
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