Nonheme iron enzymes are known to oxidize a range of substrates by catalyzing the activation of dioxygen. The Fe(IV)-oxido species are generally believed to be key reactive intermediates in nonheme iron enzymes for performing different transformations like halogenation, hydroxylation, olefin epoxidation etc. Spectroscopic studies implicate high-valent diiron species as intermediates in the oxidation chemistry of the diiron centers in methane monooxygenase (MMO) and ribonucleotide reductase (RNR), while mononuclear Fe(IV)-oxido units have been proposed as the oxidant for several mononuclear nonheme iron enzymes.1 The bispidine iron(IV)oxido species trans-N3-[(L)FeIV=O(Cl)]+ (S=1) is the most reactive nonheme iron model system known so far, with a reactivity similar to nonheme iron enzymes (C-H abstraction at cyclohexane, -80°C (propionitrile), t1/2 = 3.5 sec), and with 100% selectivity produces cyclohexyl chloride.2 In absence of organic substrates, there are various self-decay pathways, one leading to an oxido-bridged diiron(III) species. The reactivity of this “resting state” as well as reasons for the unprecedented reactivity of trans-N3-[(L)FeIV=O(Cl)]+ are discussed on the basis of spectroscopic study (see scheme 1).3
[L(Cl)FeIII-O-FeIII(Cl)L]2+
Scheme 1: Proposed mechanism of oxidation with high-valent iron-bispidine complexes.
Figure 1: Time-dep. Formation and decay of [L(Cl)FeIV=O]+ and decay with cyclohexane.