TY - JOUR
T1 - HFEPR and Computational Studies on the Electronic Structure of a High-Spin Oxidoiron(IV) Complex in Solution
AU - Bucinsky, Lukas
AU - Rohde, Gregory T.
AU - Que, Lawrence
AU - Ozarowski, Andrew
AU - Krzystek, J.
AU - Breza, Martin
AU - Telser, Joshua
N1 - Publisher Copyright:
© 2016 American Chemical Society.
PY - 2016/5/2
Y1 - 2016/5/2
N2 - Nonheme iron enzymes perform diverse and important functions in biochemistry. The active form of these enzymes comprises the ferryl, oxidoiron(IV), [FeO]2+ unit. In enzymes, this unit is in the high-spin, quintet, S = 2, ground state, while many synthetic model compounds exist in the spin triplet, S = 1, ground state. Recently, however, Que and co-workers reported an oxidoiron(IV) complex with a quintet ground state, [FeO(TMG3tren)](OTf)2, where TMG3tren = 1,1,1-tris{2-[N2-(1,1,3,3-tetramethylguanidino)]ethyl}amine and OTf = CF3SO3-. The trigonal geometry imposed by this ligand, as opposed to the tetragonal geometry of earlier model complexes, favors the high-spin ground state. Although [FeO(TMG3tren)]2+ has been earlier probed by magnetic circular dichroism (MCD) and Mössbauer spectroscopies, the technique of high-frequency and -field electron paramagnetic resonance (HFEPR) is superior for describing the electronic structure of the iron(IV) center because of its ability to establish directly the spin-Hamiltonian parameters of high-spin metal centers with high precision. Herein we describe HFEPR studies on [FeO(TMG3tren)](OTf)2 generated in situ and confirm the S = 2 ground state with the following parameters: D = +4.940(5) cm-1, E = 0.000(5), B40 = -14(1) × 10-4 cm-1, g⊥ = 2.006(2), and g∥ = 2.03(2). Extraction of a fourth-order spin-Hamiltonian parameter is unusual for HFEPR and impossible by other techniques. These experimental results are combined with state-of-the-art computational studies along with previous structural and spectroscopic results to provide a complete picture of the electronic structure of this biomimetic complex. Specifically, the calculations reproduce well the spin-Hamiltonian parameters of the complex, provide a satisfying geometrical picture of the S = 2 oxidoiron(IV) moiety, and demonstrate that the TMG3tren is an "innocent" ligand.
AB - Nonheme iron enzymes perform diverse and important functions in biochemistry. The active form of these enzymes comprises the ferryl, oxidoiron(IV), [FeO]2+ unit. In enzymes, this unit is in the high-spin, quintet, S = 2, ground state, while many synthetic model compounds exist in the spin triplet, S = 1, ground state. Recently, however, Que and co-workers reported an oxidoiron(IV) complex with a quintet ground state, [FeO(TMG3tren)](OTf)2, where TMG3tren = 1,1,1-tris{2-[N2-(1,1,3,3-tetramethylguanidino)]ethyl}amine and OTf = CF3SO3-. The trigonal geometry imposed by this ligand, as opposed to the tetragonal geometry of earlier model complexes, favors the high-spin ground state. Although [FeO(TMG3tren)]2+ has been earlier probed by magnetic circular dichroism (MCD) and Mössbauer spectroscopies, the technique of high-frequency and -field electron paramagnetic resonance (HFEPR) is superior for describing the electronic structure of the iron(IV) center because of its ability to establish directly the spin-Hamiltonian parameters of high-spin metal centers with high precision. Herein we describe HFEPR studies on [FeO(TMG3tren)](OTf)2 generated in situ and confirm the S = 2 ground state with the following parameters: D = +4.940(5) cm-1, E = 0.000(5), B40 = -14(1) × 10-4 cm-1, g⊥ = 2.006(2), and g∥ = 2.03(2). Extraction of a fourth-order spin-Hamiltonian parameter is unusual for HFEPR and impossible by other techniques. These experimental results are combined with state-of-the-art computational studies along with previous structural and spectroscopic results to provide a complete picture of the electronic structure of this biomimetic complex. Specifically, the calculations reproduce well the spin-Hamiltonian parameters of the complex, provide a satisfying geometrical picture of the S = 2 oxidoiron(IV) moiety, and demonstrate that the TMG3tren is an "innocent" ligand.
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U2 - 10.1021/acs.inorgchem.6b00169
DO - 10.1021/acs.inorgchem.6b00169
M3 - Article
C2 - 27031000
AN - SCOPUS:84966429123
SN - 0020-1669
VL - 55
SP - 3933
EP - 3945
JO - Inorganic Chemistry
JF - Inorganic Chemistry
IS - 8
ER -