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This theoretical work addresses the mechanistic switch between hydroxylase (alcohol formation) and desaturase (olefin formation) activities during alkane oxidation by two non-heme high-valent oxoiron reagents, the enzyme taurine:α-ketoglutarase dioxygenase (TauD) and the synthetic shape-selective catalyst (TpOBzFe), toward cyclohexadiene, cyclohexane, cyclopentane, and ethane. As we show, the desaturase/hydroxylase steps obey unique orbital selection rules, and the mechanistic switch is determined by intrinsic reactivity factors that depend on the ligand-sphere flexibility of the oxoiron species, the substrate, and the spin states of the reaction pathways. Testable predictions are outlined.


Dandamudi Usharani, Deepa Janardanan, Sason Shaik. Does the TauD enzyme always hydroxylate alkanes, while an analogous synthetic non-heme reagent always desaturates them? Journal of the American Chemical Society. 2011 Jan 19;133(2):176-9

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PMID: 21171573

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