Calcium dissolution in bridgmanite in the Earth's deep mantle.

Accurate knowledge of the mineralogy is essential for understanding the lower mantle, which represents more than half of Earth's volume. CaSiO3 perovskite is believed to be the third-most-abundant mineral throughout the lower mantle, following bridgmanite and ferropericlase1-3. Here we experimentally show that the calcium solubility in bridgmanite increases steeply at about 2,300 kelvin and above 40 gigapascals to a level sufficient for a complete dissolution of all CaSiO3 component in pyrolite into bridgmanite, resulting in the disappearance of CaSiO3 perovskite at depths greater than about 1,800 kilometres along the geotherm4,5. Hence we propose a change from a two-perovskite domain (TPD; bridgmanite plus CaSiO3 perovskite) at the shallower lower mantle to a single-perovskite domain (SPD; calcium-rich bridgmanite) at the deeper lower mantle. Iron seems to have a key role in increasing the calcium solubility in bridgmanite. The temperature-driven nature can cause large lateral variations in the depth of the TPD-to-SPD change in response to temperature variations (by more than 500 kilometres). Furthermore, the SPD should have been thicker in the past when the mantle was warmer. Our finding requires revision of the deep-mantle mineralogy models and will have an impact on our understanding of the composition, structure, dynamics and evolution of the region.

Stabilization of a Heme-HNO Model Complex Using a Bulky Bis-Picket Fence Porphyrin and Reactivity Studies with NO.

Nitroxyl, HNO/NO-, the one-electron reduced form of NO, is suggested to take part in distinct signaling pathways in mammals and is also a key intermediate in various heme-catalyzed NOx interconversions in the nitrogen cycle. Cytochrome P450nor (Cyt P450nor) is a heme-containing enzyme that performs NO reduction to N2O in fungal denitrification. The reactive intermediate in this enzyme, termed "Intermediate I", is proposed to be an Fe-NHO/Fe-NHOH type species, but it is difficult to study its electronic structure and exact protonation state due to its instability. Here, we utilize a bulky bis-picket fence porphyrin to obtain the first stable heme-HNO model complex, [Fe(3,5-Me-BAFP)(MI)(NHO)], as a model for Intermediate I, and more generally HNO adducts of heme proteins. Due to the steric hindrance of the bis-picket fence porphyrin, [Fe(3,5-Me-BAFP)(MI)(NHO)] is stable (τ1/2 = 56 min at -30 °C), can be isolated as a solid, and is available for thorough spectroscopic characterization. In particular, we were able to solve a conundrum in the literature and provide the first full vibrational characterization of a heme-HNO complex using IR and nuclear resonance vibrational spectroscopy (NRVS). Reactivity studies of [Fe(3,5-Me-BAFP)(MI)(NHO)] with NO gas show a 91 ± 10% yield for N2O formation, demonstrating that heme-HNO complexes are catalytically competent intermediates for NO reduction to N2O in Cyt P450nor. The implications of these results for the mechanism of Cyt P450nor are further discussed.

What Is the Right Level of Activation of a High-Spin {FeNO}7 Complex to Enable Direct N-N Coupling? Mechanistic Insight into Flavodiiron NO Reductases.

Flavodiiron nitric oxide reductases (FNORs), found in pathogenic bacteria, are capable of reducing nitric oxide (NO) to nitrous oxide (N2O) to detoxify NO released by the human immune system. Previously, we reported the first FNOR model system that mediates direct NO reduction (Dong, H. T.; J. Am. Chem. Soc. 2018, 140, 13429-13440), but no intermediate of the reaction could be characterized. Here, we present a new set of model complexes that, depending on the ligand substitution, can either mediate direct NO reduction or stabilize a highly activated high-spin (hs) {FeNO}7 complex, the first intermediate of the reaction. The precursors, [{FeII(MPA-(RPhO)2)}2] (1, R = H and 2, R = tBu, Me), were prepared first and fully characterized. Complex 1 (without steric protection) directly reduces NO to N2O almost quantitatively, which constitutes only the second example of this reaction in model systems. Contrarily, the reaction of sterically protected 2 with NO forms the stable mononitrosyl complex 3, which shows one of the lowest N-O stretching frequencies (1689 cm-1) observed so far for a mononuclear hs-{FeNO}7 complex. This study confirms that an N-O stretch ≤1700 cm-1 represents the appropriate level of activation of the FeNO unit to enable direct NO reduction. The higher activation level of these hs-{FeNO}7 complexes required for NO reduction compared to those formed in FNORs emphasizes the importance of hydrogen bonding residues in the active sites of FNORs to activate the bound NO ligands for direct N-N coupling and N2O formation. The implications of these results for FNORs are further discussed.

Distortion of the [FeNO]2 Core in Flavodiiron Nitric Oxide Reductase Models Inhibits N-N Bond Formation and Promotes Formation of Unusual Dinitrosyl Iron Complexes: Implications for Catalysis and Reactivity.

Flavodiiron nitric oxide reductases (FNORs) carry out the reduction of nitric oxide (NO) to nitrous oxide (N2O), allowing infectious pathogens to mitigate toxic levels of NO generated in the human immune response. We previously reported the model complex [Fe2(BPMP)(OPr)(NO)2](OTf)2 (1, OPr- = propionate) that contains two coplanar NO ligands and that is capable of quantitative NO reduction to N2O [White et al. J. Am. Chem. Soc. 2018, 140, 2562-2574]. Here we investigate, for the first time, how a distortion of the active site affects the ability of the diiron core to mediate N2O formation. For this purpose, we prepared several analogues of 1 that contain two monodentate ligands in place of the bridging carboxylate, [Fe2(BPMP)(X)2(NO)2]3+/1+ (2-X; X = triflate, 1-methylimidazole, or methanol). Structural data of 2-X show that without the bridging carboxylate, the diiron core expands, leading to elongated (O)N-N(O) distances (from 2.80 Å in 1 to 3.00-3.96 Å in 2-X) and distorted (O)N-Fe-Fe-N(O) dihedral angles (from coplanarity (5.9°) in 1 to 52.9-85.1° in 2-X). Whereas 1 produces quantitative amounts of N2O upon one-electron reduction, N2O production is substantially impeded in 2-X, to an initial 5-10% N2O yield. The main products after reduction are unprecedented hs-FeII/{Fe(NO)2}9/10 dinitrosyl iron complexes (DNICs). Even though mononuclear DNICs are stable and do not show N-N coupling (since it is a spin-forbidden process), the hs-FeII/{Fe(NO)2}9/10 DNICs obtained from 2-X show unexpected reactivity and produce up to quantitative N2O yields after 2 h. The implications of these results for the active site structure of FNORs are discussed.

High-throughput nuclear resonance time domain interferometry using annular slits.

Nuclear resonance time domain interferometry (NR-TDI) is used to study the slow dynamics of liquids (that do not require Mössbauer isotopes) at atomic and molecular length scales. Here the TDI method of using a stationary two-line magnetized 57Fe foil as a source and a stationary single-line stainless steel foil analyzer is employed. The new technique of adding an annular slit in front of a single silicon avalanche photodiode detector enables a wide range of momentum transfers (1 to 100 nm-1 by varying the distance between the annular slits and sample) with a high count rate of up to 160 Hz with a Δq resolution of ±1.7 nm-1 at q = 14 nm-1. The sensitivity of this method in determining relaxation times is quantified and discussed. The Kohlrausch-Williams-Watts (KWW) model was used to extract relaxation times for glycerol. These relaxation times give insight into the dynamics of the electron density fluctuations of glycerol as a function of temperature and momentum transfers.

Structural characterization of a non-heme iron active site in zeolites that hydroxylates methane.

Iron-containing zeolites exhibit unprecedented reactivity in the low-temperature hydroxylation of methane to form methanol. Reactivity occurs at a mononuclear ferrous active site, α-Fe(II), that is activated by N2O to form the reactive intermediate α-O. This has been defined as an Fe(IV)=O species. Using nuclear resonance vibrational spectroscopy coupled to X-ray absorption spectroscopy, we probe the bonding interaction between the iron center, its zeolite lattice-derived ligands, and the reactive oxygen. α-O is found to contain an unusually strong Fe(IV)=O bond resulting from a constrained coordination geometry enforced by the zeolite lattice. Density functional theory calculations clarify how the experimentally determined geometric structure of the active site leads to an electronic structure that is highly activated to perform H-atom abstraction.

Mechanism of selective benzene hydroxylation catalyzed by iron-containing zeolites.

A direct, catalytic conversion of benzene to phenol would have wide-reaching economic impacts. Fe zeolites exhibit a remarkable combination of high activity and selectivity in this conversion, leading to their past implementation at the pilot plant level. There were, however, issues related to catalyst deactivation for this process. Mechanistic insight could resolve these issues, and also provide a blueprint for achieving high performance in selective oxidation catalysis. Recently, we demonstrated that the active site of selective hydrocarbon oxidation in Fe zeolites, named α-O, is an unusually reactive Fe(IV)=O species. Here, we apply advanced spectroscopic techniques to determine that the reaction of this Fe(IV)=O intermediate with benzene in fact regenerates the reduced Fe(II) active site, enabling catalytic turnover. At the same time, a small fraction of Fe(III)-phenolate poisoned active sites form, defining a mechanism for catalyst deactivation. Density-functional theory calculations provide further insight into the experimentally defined mechanism. The extreme reactivity of α-O significantly tunes down (eliminates) the rate-limiting barrier for aromatic hydroxylation, leading to a diffusion-limited reaction coordinate. This favors hydroxylation of the rapidly diffusing benzene substrate over the slowly diffusing (but more reactive) oxygenated product, thereby enhancing selectivity. This defines a mechanism to simultaneously attain high activity (conversion) and selectivity, enabling the efficient oxidative upgrading of inert hydrocarbon substrates.

Pressure-Induced Collapse of Magnetic Order in Jarosite.

We report a pressure-induced phase transition in the frustrated kagomé material jarosite at ∼45 GPa, which leads to the disappearance of magnetic order. Using a suite of experimental techniques, we characterize the structural, electronic, and magnetic changes in jarosite through this phase transition. Synchrotron powder x-ray diffraction and Fourier transform infrared spectroscopy experiments, analyzed in aggregate with the results from density functional theory calculations, indicate that the material changes from a R3[over ¯]m structure to a structure with a R3[over ¯]c space group. The resulting phase features a rare twisted kagomé lattice in which the integrity of the equilateral Fe^{3+} triangles persists. Based on symmetry arguments we hypothesize that the resulting structural changes alter the magnetic interactions to favor a possible quantum paramagnetic phase at high pressure.

Exploring the Limits of Dative Boratrane Bonding: Iron as a Strong Lewis Base in Low-Valent Non-Heme Iron-Nitrosyl Complexes.

We previously reported the synthesis and preliminary characterization of a unique series of low-spin (ls) {FeNO}8-10 complexes supported by an ambiphilic trisphosphineborane ligand, [Fe(TPB)(NO)]+/0/-. Herein, we use advanced spectroscopic techniques and density functional theory (DFT) calculations to extract detailed information as to how the bonding changes across the redox series. We find that, in spite of the highly reduced nature of these complexes, they feature an NO+ ligand throughout with strong Fe-NO π-backbonding and essentially closed-shell electronic structures of their FeNO units. This is enabled by an Fe-B interaction that is present throughout the series. In particular, the most reduced [Fe(TPB)(NO)]- complex, an example of a ls-{FeNO}10 species, features a true reverse dative Fe → B bond where the Fe center acts as a strong Lewis-base. Hence, this complex is in fact electronically similar to the ls-{FeNO}8 system, with two additional electrons "stored" on site in an Fe-B single bond. The outlier in this series is the ls-{FeNO}9 complex, due to spin polarization (quantified by pulse EPR spectroscopy), which weakens the Fe-NO bond. These data are further contextualized by comparison with a related N2 complex, [Fe(TPB)(N2)]-, which is a key intermediate in Fe(TPB)-catalyzed N2 fixation. Our present study finds that the Fe → B interaction is key for storing the electrons needed to achieve a highly reduced state in these systems, and highlights the pitfalls associated with using geometric parameters to try to evaluate reverse dative interactions, a finding with broader implications to the study of transition metal complexes with boratrane and related ligands.

Stability of ferrous-iron-rich bridgmanite under reducing midmantle conditions.

Our current understanding of the electronic state of iron in lower-mantle minerals leads to a considerable disagreement in bulk sound speed with seismic measurements if the lower mantle has the same composition as the upper mantle (pyrolite). In the modeling studies, the content and oxidation state of Fe in the minerals have been assumed to be constant throughout the lower mantle. Here, we report high-pressure experimental results in which Fe becomes dominantly Fe2+ in bridgmanite synthesized at 40-70 GPa and 2,000 K, while it is in mixed oxidation state (Fe3+/∑Fe = 60%) in the samples synthesized below and above the pressure range. Little Fe3+ in bridgmanite combined with the strong partitioning of Fe2+ into ferropericlase will alter the Fe content for these minerals at 1,100- to 1,700-km depths. Our calculations show that the change in iron content harmonizes the bulk sound speed of pyrolite with the seismic values in this region. Our experiments support no significant changes in bulk composition for most of the mantle, but possible changes in physical properties and processes (such as viscosity and mantle flow patterns) in the midmantle.

Exploring the Vibrational Side of Spin-Phonon Coupling in Single-Molecule Magnets via 161 Dy Nuclear Resonance Vibrational Spectroscopy.

Synchrotron-based nuclear resonance vibrational spectroscopy (NRVS) using the Mössbauer isotope 161 Dy has been employed for the first time to study the vibrational properties of a single-molecule magnet (SMM) incorporating DyIII , namely [Dy(Cy3 PO)2 (H2 O)5 ]Br3 ⋅2 (Cy3 PO)⋅2 H2 O ⋅2 EtOH. The experimental partial phonon density of states (pDOS), which includes all vibrational modes involving a displacement of the DyIII ion, was reproduced by means of simulations using density functional theory (DFT), enabling the assignment of all intramolecular vibrational modes. This study proves that 161 Dy NRVS is a powerful experimental tool with significant potential to help to clarify the role of phonons in SMMs.

Synthetic Model Complex of the Key Intermediate in Cytochrome P450 Nitric Oxide Reductase.

Fungal denitrification plays a crucial role in the nitrogen cycle and contributes to the total N2O emission from agricultural soils. Here, cytochrome P450 NO reductase (P450nor) reduces two NO to N2O using a single heme site. Despite much research, the exact nature of the critical "Intermediate I" responsible for the key N-N coupling step in P450nor is unknown. This species likely corresponds to a Fe-NHOH-type intermediate with an unknown electronic structure. Here we report a new strategy to generate a model system for this intermediate, starting from the iron(III) methylhydroxylamide complex [Fe(3,5-Me-BAFP)(NHOMe)] (1), which was fully characterized by 1H NMR, UV-vis, electron paramagnetic resonance, and vibrational spectroscopy (rRaman and NRVS). Our data show that 1 is a high-spin ferric complex with an N-bound hydroxylamide ligand that is strongly coordinated (Fe-N distance, 1.918 Å; Fe-NHOMe stretch, 558 cm-1). Simple one-electron oxidation of 1 at -80 °C then cleanly generates the first model system for Intermediate I, [Fe(3,5-Me-BAFP)(NHOMe)]+ (1+). UV-vis, resonance Raman, and Mössbauer spectroscopies, in comparison to the chloro analogue [Fe(3,5-Me-BAFP)(Cl)]+, demonstrate that 1+ is best described as an FeIII-(NHOMe)• complex with a bound NHOMe radical. Further reactivity studies show that 1+ is highly reactive toward NO, a reaction that likely proceeds via N-N bond formation, following a radical-radical-type coupling mechanism. Our results therefore provide experimental evidence, for the first time, that an FeIII-(NHOMe)• electronic structure is indeed a reasonable electronic description for Intermediate I and that this electronic structure is advantageous for P450nor catalysis because it can greatly facilitate N-N bond formation and, ultimately, N2O generation.

Electronic Structures of an [Fe(NNR2)]+/0/- Redox Series: Ligand Noninnocence and Implications for Catalytic Nitrogen Fixation.

The intermediacy of metal-NNH2 complexes has been implicated in the catalytic cycles of several examples of transition-metal-mediated nitrogen (N2) fixation. In this context, we have shown that triphosphine-supported Fe(N2) complexes can be reduced and protonated at the distal N atom to yield Fe(NNH2) complexes over an array of charge and oxidation states. Upon exposure to further H+/e- equivalents, these species either continue down a distal-type Chatt pathway to yield a terminal iron(IV) nitride or instead follow a distal-to-alternating pathway resulting in N-H bond formation at the proximal N atom. To understand the origin of this divergent selectivity, herein we synthesize and elucidate the electronic structures of a redox series of Fe(NNMe2) complexes, which serve as spectroscopic models for their reactive protonated congeners. Using a combination of spectroscopies, in concert with density functional theory and correlated ab initio calculations, we evidence one-electron redox noninnocence of the "NNMe2" moiety. Specifically, although two closed-shell configurations of the "NNR2" ligand have been commonly considered in the literature-isodiazene and hydrazido(2-)-we provide evidence suggesting that, in their reduced forms, the present iron complexes are best viewed in terms of an open-shell [NNR2]•- ligand coupled antiferromagnetically to the Fe center. This one-electron redox noninnocence resembles that of the classically noninnocent ligand NO and may have mechanistic implications for selectivity in N2 fixation activity.

Stable Ferrous Mononitroxyl {FeNO}8 Complex with a Hindered Hydrotris(pyrazolyl)borate Coligand: Structure, Spectroscopic Characterization, and Reactivity Toward NO and O2.

The iron(II)-nitroxyl complex [Fe(NO)(L3)] (1) (with L3- = a hindered hydrotris(pyrazolyl)borate ligand), a high-spin (hs)-{FeNO}8 complex in the Enemark-Feltham notation, is surprisingly stable and is the first of its kind that could be structurally characterized. We further studied this compound using a variety of spectroscopic methods. These results indicate a hs iron(II) center with a bound 3NO- ligand where the spins are antiferromagnetic coupled ( St = 1). Vibrational data show that this complex has a very strong Fe-NO bond. DFT calculations support this result and link it to very strong π-donation from the 3NO- ligand to the iron(II) center. Furthermore, a very unusual equilibrium between the hs-{FeNO}8 complex and a dinitrosyl iron complex (DNIC) of {Fe(NO)2}9 type is observed. The O2 reactivity of the complex is finally reported.

Elucidation of the Fe(IV)=O intermediate in the catalytic cycle of the halogenase SyrB2.

Mononuclear non-haem iron (NHFe) enzymes catalyse a broad range of oxidative reactions, including halogenation, hydroxylation, ring closure, desaturation and aromatic ring cleavage reactions. They are involved in a number of biological processes, including phenylalanine metabolism, the production of neurotransmitters, the hypoxic response and the biosynthesis of secondary metabolites. The reactive intermediate in the catalytic cycles of these enzymes is a high-spin S = 2 Fe(IV)=O species, which has been trapped for a number of NHFe enzymes, including the halogenase SyrB2 (syringomycin biosynthesis enzyme 2). Computational studies aimed at understanding the reactivity of this Fe(IV)=O intermediate are limited in applicability owing to the paucity of experimental knowledge about its geometric and electronic structure. Synchrotron-based nuclear resonance vibrational spectroscopy (NRVS) is a sensitive and effective method that defines the dependence of the vibrational modes involving Fe on the nature of the Fe(IV)=O active site. Here we present NRVS structural characterization of the reactive Fe(IV)=O intermediate of a NHFe enzyme, namely the halogenase SyrB2 from the bacterium Pseudomonas syringae pv. syringae. This intermediate reacts via an initial hydrogen-atom abstraction step, performing subsequent halogenation of the native substrate or hydroxylation of non-native substrates. A correlation of the experimental NRVS data to electronic structure calculations indicates that the substrate directs the orientation of the Fe(IV)=O intermediate, presenting specific frontier molecular orbitals that can activate either selective halogenation or hydroxylation.

161 Dy Time-Domain Synchrotron Mössbauer Spectroscopy for Investigating Single-Molecule Magnets Incorporating Dy Ions.

Time-domain synchrotron Mössbauer spectroscopy (SMS) based on the Mössbauer effect of 161 Dy has been used to investigate the magnetic properties of a DyIII -based single-molecule magnet (SMM). The magnetic hyperfine field of [Dy(Cy3 PO)2 (H2 O)5 ]Br3 ⋅2 (Cy3 PO)⋅2 H2 O⋅2 EtOH is with B0 =582.3(5) T significantly larger than that of the free-ion DyIII with a 6 H15/2 ground state. This difference is attributed to the influence of the coordinating ligands on the Fermi contact interaction between the s and 4f electrons of the DyIII ion. This study demonstrates that 161 Dy SMS is an effective local probe of the influence of the coordinating ligands on the magnetic structure of Dy-containing compounds.

Non-heme High-Spin {FeNO}6-8 Complexes: One Ligand Platform Can Do It All.

Heme and non-heme iron-nitrosyl complexes are important intermediates in biology. While there are numerous examples of low-spin heme iron-nitrosyl complexes in different oxidation states, much less is known about high-spin (hs) non-heme iron-nitrosyls in oxidation states other than the formally ferrous NO adducts ({FeNO}7 in the Enemark-Feltham notation). In this study, we present a complete series of hs-{FeNO}6-8 complexes using the TMG3tren coligand. Redox transformations from the hs-{FeNO}7 complex [Fe(TMG3tren)(NO)]2+ to its {FeNO}6 and {FeNO}8 analogs do not alter the coordination environment of the iron center, allowing for detailed comparisons between these species. Here, we present new MCD, NRVS, XANES/EXAFS, and Mössbauer data, demonstrating that these redox transformations are metal based, which allows us to access hs-Fe(II)-NO-, Fe(III)-NO-, and Fe(IV)-NO- complexes. Vibrational data, analyzed by NCA, directly quantify changes in Fe-NO bonding along this series. Optical data allow for the identification of a "spectator" charge-transfer transition that, together with Mössbauer and XAS data, directly monitors the electronic changes of the Fe center. Using EXAFS, we are also able to provide structural data for all complexes. The magnetic properties of the complexes are further analyzed (from magnetic Mössbauer). The properties of our hs-{FeNO}6-8 complexes are then contrasted to corresponding, low-spin iron-nitrosyl complexes where redox transformations are generally NO centered. The hs-{FeNO}8 complex can further be protonated by weak acids, and the product of this reaction is characterized. Taken together, these results provide unprecedented insight into the properties of biologically relevant non-heme iron-nitrosyl complexes in three relevant oxidation states.

The Semireduced Mechanism for Nitric Oxide Reduction by Non-Heme Diiron Complexes: Modeling Flavodiiron Nitric Oxide Reductases.

Flavodiiron nitric oxide reductases (FNORs) are a subclass of flavodiiron proteins (FDPs) capable of preferential binding and subsequent reduction of NO to N2O. FNORs are found in certain pathogenic bacteria, equipping them with resistance to nitrosative stress, generated as a part of the immune defense in humans, and allowing them to proliferate. Here, we report the spectroscopic characterization and detailed reactivity studies of the diiron dinitrosyl model complex [Fe2(BPMP)(OPr)(NO)2](OTf)2 for the FNOR active site that is capable of reducing NO to N2O [Zheng et al., J. Am. Chem. Soc. 2013, 135, 4902-4905]. Using UV-vis spectroscopy, cyclic voltammetry, and spectro-electrochemistry, we show that one reductive equivalent is in fact sufficient for the quantitative generation of N2O, following a semireduced reaction mechanism. This reaction is very efficient and produces N2O with a first-order rate constant k > 102 s-1. Further isotope labeling studies confirm an intramolecular N-N coupling mechanism, consistent with the rapid time scale of the reduction and a very low barrier for N-N bond formation. Accordingly, the reaction proceeds at -80 °C, allowing for the direct observation of the mixed-valent product of the reaction. At higher temperatures, the initial reaction product is unstable and decays, ultimately generating the diferrous complex [Fe2(BPMP)(OPr)2](OTf) and an unidentified ferric product. These results combined offer deep insight into the mechanism of NO reduction by the relevant model complex [Fe2(BPMP)(OPr)(NO)2]2+ and provide direct evidence that the semireduced mechanism would constitute a highly efficient pathway to accomplish NO reduction to N2O in FNORs and in synthetic catalysts.

Impact of Pressure on Magnetic Order in Jarosite.

Jarosite, a mineral with a kagomé lattice, displays magnetic frustration yet orders magnetically below 65 K. As magnetic frustration can engender exotic physical properties, understanding the complex magnetism of jarosite comprises a multidecade interdisciplinary challenge. Unraveling the nature of the disparate magnetic coupling interactions that lead to magnetic order in jarosite remains an open question. Specifically, there is no observed trend in the interlayer spacing with magnetic order. Similarly, the relationship between metal-ligand bond distance and magnetic order remains uninvestigated. Here, we use applied pressure to smoothly vary jarosite's structure without manipulating the chemical composition, enabling a chemically invariant structure-function study. Using single-crystal and powder X-ray diffraction, we show that high applied pressures alter both the interlayer spacing and the metal-ligand bond distances. By harnessing a suite of magnetic techniques under pressure, including SQUID-based magnetometry, time-resolved synchrotron Mössbauer spectroscopy, and X-ray magnetic circular dichroism, we construct the magnetic phase diagram for jarosite up to 40 GPa. Notably, we demonstrate that the magnetic ordering temperature increases dramatically to 240 K at the highest pressures. Additionally, we conduct X-ray emission spectroscopy, Mössbauer spectroscopy, and UV-visible absorption spectroscopy experiments to comprehensively map the magnetic and electronic structures of jarosite at high pressure. We use these maps to construct chemically pure magnetostructural correlations which fully explain the nature and role of the disparate magnetic coupling interactions in jarosite.

Nuclear Resonance Vibrational Spectroscopy Definition of O2 Intermediates in an Extradiol Dioxygenase: Correlation to Crystallography and Reactivity.

The extradiol dioxygenases are a large subclass of mononuclear nonheme Fe enzymes that catalyze the oxidative cleavage of catechols distal to their OH groups. These enzymes are important in bioremediation, and there has been significant interest in understanding how they activate O2. The extradiol dioxygenase homoprotocatechuate 2,3-dioxygenase (HPCD) provides an opportunity to study this process, as two O2 intermediates have been trapped and crystallographically defined using the slow substrate 4-nitrocatechol (4NC): a side-on Fe-O2-4NC species and a Fe-O2-4NC peroxy bridged species. Also with 4NC, two solution intermediates have been trapped in the H200N variant, where H200 provides a second-sphere hydrogen bond in the wild-type enzyme. While the electronic structure of these solution intermediates has been defined previously as FeIII-superoxo-catecholate and FeIII-peroxy-semiquinone, their geometric structures are unknown. Nuclear resonance vibrational spectroscopy (NRVS) is an important tool for structural definition of nonheme Fe-O2 intermediates, as all normal modes with Fe displacement have intensity in the NRVS spectrum. In this study, NRVS is used to define the geometric structure of the H200N-4NC solution intermediates in HPCD as an end-on FeIII-superoxo-catecholate and an end-on FeIII-hydroperoxo-semiquinone. Parallel calculations are performed to define the electronic structures and protonation states of the crystallographically defined wild-type HPCD-4NC intermediates, where the side-on intermediate is found to be a FeIII-hydroperoxo-semiquinone. The assignment of this crystallographic intermediate is validated by correlation to the NRVS data through computational removal of H200. While the side-on hydroperoxo semiquinone intermediate is computationally found to be nonreactive in peroxide bridge formation, it is isoenergetic with a superoxo catecholate species that is competent in performing this reaction. This study provides insight into the relative reactivities of FeIII-superoxo and FeIII-hydroperoxo intermediates in nonheme Fe enzymes and into the role H200 plays in facilitating extradiol catalysis.