Abstract
Mononuclear non-heme iron (NHFe) enzymes catalyze a number of key biological reactions including hydroxylation, desaturation, ring closure and halogenation.[1-3] The reactive intermediate that carries out many of the C–H bond activations is an S = 2 FeIV=O species that has been observed and characterized in several enzyme systems.[3-5] Synthetic efforts have yielded FeIV=O model complexes that exhibit an S = 1 ground state[6, 7] in all but three cases: (H2O)5FeIV=O[8], (H3buea)FeIV=O[9] and (TMG3tren)FeIV=O (1).[10] 1 has an FeIV=O unit ligated by TMG3tren in a C3ν trigonal bipyramidal geometry (Figure 1A), and an S = 2 ground state replicating that of enzyme intermediates.[10, 11] 1 is reactive in oxo-atom transfer and H-atom abstraction, but in the latter it is only as reactive as the approximately-C4v S = 1 (N4Py)FeIV=O (2, Figure 1B) complex where both have the same reaction rate with 1,4-cyclohexadiene (CHD).[10] Original studies from our group showed that whereas S = 1 reaction coordinates only have a □-attack pathway, involving the β-d□* orbital, available for electrophilic reactivity, S = 2 systems are predicted to possess an additional -attack pathway involving the ⟨-dz2 orbital that is lowered in energy due to spin-polarization.[12, 13] This has recently been referred to as an exchange enhancement.[14] In this study, we utilize Nuclear Resonance Vibrational Spectroscopy (NRVS) to obtain ground-state vibrational data on 1 for comparison to 2[15] and, through correlations to DFT calculations, to understand the observed similar reactivities of 1 (S = 2) and 2 (S = 1). These studies define the steric and intrinsic electronic contributions to the reaction barriers and establish that both the S = 1 and S = 2 surfaces have significant steric contributions due to the different directionalities of substrate approach and thus similar intrinsic reactivities.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.