The crystal structure of a high-Spin oxoiron(IV) complex and characterization of Its self-Decay pathway

[Fe^IV(O)(TMG₃tren)]²⁺ (1 ; TMG ₃tren = 1,1,1 -tris{2-N²-(1,1,3,3-tetramethylguanidino)] ethyl}amine) is a unique example of an isolable synthetic S = 2 oxoiron(IV) complex, which serves as a model for the hlgh-valent oxoiron(IV) intermediates observed In nonheme iron enzymes. Congruent with DFT calculations predicting a more reactive S = 2 oxoiron(IV) center, 1 has a lifetime significantly shorter than those of related S = 1 oxolron(IV) complexes. The self-decay of 1 exhibits strictly first-order kinetic behavior and is unaffected by solvent deuteration, suggesting an intramolecular process. This hypothesis was supported by ESI-MS analysis of the iron products and a significant retardation of self-decay upon use of a perdeuteromethyl TMG₃tren isotopomer, d₃₆-1 (KIE = 24 at 25 °C). The greatly enhanced thermal stability of d₃₆-1 allowed growth of diffraction quality crystals for which a high-resolution crystal structure was obtained. This structure showed an Fe=O unit (r= 1.661 (2) Å) in the intended trigonal bipyramidal geometry enforced by the sterically bulky tetramethylguanidinyl donors of the tetradentate tripodal TMG₃tren ligand. The close proximity of the methyl substituents to the oxoiron unit yielded three symmetrically oriented short C-D⋯O nonbonded contacts (2.38-2.49 Å), an arrangement that facilitated self-decay by rate-determining intramolecular hydrogen atom abstraction and subsequent formation of a ligand-hydroxylated iron(III) product. EPR and Mössbauer quantification of the various iron products, referenced against those obtained from reaction of 1 with 1,4-cyclohexadiene, allowed formulation of a detailed mechanism for the self-decay process. The solution of this first crystal structure of a high-spin (S = 2) oxoiron(IV) center represents a fundamental step on the path toward a full understanding of these pivotal biological intermediates.