A More Reactive Trigonal-Bipyramidal High-Spin Oxoiron(IV) Complex with a cis-Labile Site

England, Jason; Guo, Yisong; Heuvelen, Katherine M. Van; Cranswick, Matthew A.; Rohde, Gregory T.; Bominaar, Emile L.; Münck, Eckard; Que, Lawrence

doi:10.1021/ja2040909

Cited by 121 publications

(116 citation statements)

References 38 publications

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“…[136] Moreover, it was demonstrated that S = 2 state models show only comparable (or even lower) reactivity towards OAT or HAA. [202,203,204,205] These observations emphasized the need for the correlation of reactivity with electronic structure as well as the geometric and steric properties of a complex. The study of Sastri et al [174] provided a comprehensive correlation between the electronic structure properties (reflected by the reduction potentials) and reactivity.…”

Section: Mononuclear Ferryl Active Sitementioning

confidence: 99%

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

et al. 2016

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In this minireview, we provide an account of the current state-of-the-art developments in the area of mono-and binuclear non-heme enzymes (NHFe and NHFe2) and the smaller NHFe(2) synthetic models, mostly from a theoretical and computational perspective. The sheer complexity, and at the same time the beauty, of the NHFe(2) world represent a challenge for both experimental as well as theoretical methods. We emphasize that the concerted progress on both theoretical and experimental side is a conditio sine qua non for future understanding, exploration and utilization of the NHFe(2) systems.After briefly discussing the current challenges and advances in the computational methodology, we review the recent spectroscopic and computational studies of NHFe(2) enzymatic and inorganic systems and highlight the correlations between various experimental data (spectroscopic, kinetic, thermodynamic, electrochemical) and computations. Throughout, we attempt to keep in mind the most fascinating and attractive phenomenon in the NHFe(2) chemistry which is the fact that despite the strong oxidative power of many reactive intermediates, the NHFe(2) enzymes perform catalysis with high selectivity. We conclude with our personal viewpoint and hope that further developments in quantum chemistry and especially in the field of multireference wave function methods are needed to have a solid theoretical basis for the NHFe(2) studies, mostly by providing benchmarking and calibration of the computationally efficient and easy-to-use DFT methods.

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Section: Mononuclear Ferryl Active Sitementioning

confidence: 99%

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

et al. 2016

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“…A series of intermediate-spin S ¼ 1 Fe IV ═O model complexes, supported by amine, pyridine, and deprotonated amido ligands, has become available for structural, reactivity, and spectroscopic investigations (7)(8)(9)(10)(11)(12)(13). Recently, high-spin S ¼ 2 Fe IV ═O complexes have also become available, with two being structurally defined (14)(15)(16)(17)(18)(19)(20), but notably their reactivity does not surpass that of the most reactive S ¼ 1 complexes (15,18,21).…”

Section: S ¼ 2 Fementioning

confidence: 99%

π-Frontier molecular orbitals in S = 2 ferryl species and elucidation of their contributions to reactivity

Srnec

Wong

England

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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155

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S ¼ 2 FeIV ═O species are key intermediates in the catalysis of most nonheme iron enzymes. This article presents detailed spectroscopic and high-level computational studies on a structurallydefined S ¼ 2 Fe IV ═O species that define its frontier molecular orbitals, which allow its high reactivity. Importantly, there are both π-and σ-channels for reaction, and both are highly reactive because they develop dominant oxyl character at the transition state. These π-and σ-channels have different orientation dependences defining how the same substrate can undergo different reactions (H-atom abstraction vs. electrophilic aromatic attack) with Fe IV ═O sites in different enzymes, and how different substrates can undergo different reactions (hydroxylation vs. halogenation) with an Fe IV ═O species in the same enzyme.excited-state potential energy surfaces | reaction coordinates | magnetic circular dichroism | density functional calculations | multiconfigurational calculations

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“…13 While most of the Fe IV ═O model complexes have low-spin ( S = 1) ground states, 14 some models have the S = 2 spin state that is present in the enzymatic intermediates. 15 A combined spectroscopic and computational study of one of the S = 2 model complexes, (TMG 3 tren)Fe IV ═O, 15a elucidated three reactive channels available for HAA: two are active when the C–H bond is oriented perpendicular to the Fe–oxo bond ( π channels leading to S Fe = 5/2 or S Fe = 3/2 Fe III –OH intermediates) and one that is active for C–H bonds oriented along the Fe–oxo bond ( σ channel providing an S Fe III = 5/2 intermediate). 16 This is strikingly different from the S = 1 Fe IV ═O complexes, which have only one available channel, π ( S Fe III = 3/2).…”

Section: Introductionmentioning

confidence: 99%

Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity

et al. 2016

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Low temperature magnetic circular dichroism (LT MCD) spectroscopy in combination with quantum-chemical calculations are used to define the electronic structure associated with the geometric structure of the FeIV═O intermediate in SyrB2 that was previously determined by nuclear resonance vibrational spectroscopy. These studies elucidate key frontier molecular orbitals (FMOs) and their contribution to H atom abstraction reactivity. The VT MCD spectra of the enzymatic S = 2 FeIV═O intermediate with Br− ligation contain information-rich features that largely parallel the corresponding spectra of the S = 2 model complex (TMG3tren)FeIV═O (Srnec, M.; Wong, S. D.; England, J; Que, L; Solomon, E. I. Proc. Natl. Acad. Sci. USA 2012, 109, 14326–14331). However, quantitative differences are observed that correlate with π-anisotropy and oxo donor strength that perturb FMOs and affect reactivity. Due to π-anisotropy, the FeIV═O active site exhibits enhanced reactivity in the direction of the substrate cavity that proceeds through a π-channel that is controlled by perpendicular orientation of the substrate C–H bond relative to the halide–FeIV═O plane. Also, the increased intrinsic reactivity of the SyrB2 intermediate relative to the ferryl model complex is correlated to a higher oxyl character of the FeIV═O at the transition states resulting from the weaker ligand field of the halogenase.

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A More Reactive Trigonal-Bipyramidal High-Spin Oxoiron(IV) Complex with a cis-Labile Site

Cited by 121 publications

References 38 publications

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

Mono- and binuclear non-heme iron chemistry from a theoretical perspective

π-Frontier molecular orbitals in S = 2 ferryl species and elucidation of their contributions to reactivity

Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity

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