Melting and defect transitions in FeO up to pressures of Earth's core-mantle boundary.

The high-pressure melting curve of FeO controls key aspects of Earth's deep interior and the evolution of rocky planets more broadly. However, existing melting studies on wüstite were conducted across a limited pressure range and exhibit substantial disagreement. Here we use an in-situ dual-technique approach that combines a suite of >1000 x-ray diffraction and synchrotron Mössbauer measurements to report the melting curve for Fe1-xO wüstite to pressures of Earth's lowermost mantle. We further observe features in the data suggesting an order-disorder transition in the iron defect structure several hundred kelvin below melting. This solid-solid transition, suggested by decades of ambient pressure research, is detected across the full pressure range of the study (30 to 140 GPa). At 136 GPa, our results constrain a relatively high melting temperature of 4140 ± 110 K, which falls above recent temperature estimates for Earth's present-day core-mantle boundary and supports the viability of solid FeO-rich structures at the roots of mantle plumes. The coincidence of the defect order-disorder transition with pressure-temperature conditions of Earth's mantle base raises broad questions about its possible influence on key physical properties of the region, including rheology and conductivity.

The influence of δ-(Al,Fe)OOH on seismic heterogeneities in Earth's lower mantle.

The high-pressure phases of oxyhydroxides (δ-AlOOH, ε-FeOOH, and their solid solution), candidate components of subducted slabs, have wide stability fields, thus potentially influencing volatile circulation and dynamics in the Earth's lower mantle. Here, we report the elastic wave velocities of δ-(Al,Fe)OOH (Fe/(Al + Fe) = 0.13, δ-Fe13) to 79 GPa, determined by nuclear resonant inelastic X-ray scattering. At pressures below 20 GPa, a softening of the phonon spectra is observed. With increasing pressure up to the Fe3+ spin crossover (~ 45 GPa), the Debye sound velocity (vD) increases. At higher pressures, the low spin δ-Fe13 is characterized by a pressure-invariant vD. Using the equation of state for the same sample, the shear-, compressional-, and bulk-velocities (vS, vP, and vΦ) are calculated and extrapolated to deep mantle conditions. The obtained velocity data show that δ-(Al,Fe)OOH may cause low-vΦ and low-vP anomalies in the shallow lower mantle. At deeper depths, we find that this hydrous phase reproduces the anti-correlation between vS and vΦ reported for the large low seismic velocity provinces, thus serving as a potential seismic signature of hydrous circulation in the lower mantle.

Fast temperature spectrometer for samples under extreme conditions.

We have developed a multi-wavelength Fast Temperature Readout (FasTeR) spectrometer to capture a sample's transient temperature fluctuations, and reduce uncertainties in melting temperature determination. Without sacrificing accuracy, FasTeR features a fast readout rate (about 100 Hz), high sensitivity, large dynamic range, and a well-constrained focus. Complimenting a charge-coupled device spectrometer, FasTeR consists of an array of photomultiplier tubes and optical dichroic filters. The temperatures determined by FasTeR outside of the vicinity of melting are, generally, in good agreement with results from the charge-coupled device spectrometer. Near melting, FasTeR is capable of capturing transient temperature fluctuations, at least on the order of 300 K/s. A software tool, SIMFaster, is described and has been developed to simulate FasTeR and assess design configurations. FasTeR is especially suitable for temperature determinations that utilize ultra-fast techniques under extreme conditions. Working in parallel with the laser-heated diamond-anvil cell, synchrotron Mössbauer spectroscopy, and X-ray diffraction, we have applied the FasTeR spectrometer to measure the melting temperature of (57)Fe0.9Ni0.1 at high pressure.

Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c.

Cytochrome c (Cyt c) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-His (CXXCH) linker that is located in the interface region for protein-protein interactions. To determine whether the polypeptide matrix influences iron vibrational dynamics, nuclear resonance vibrational spectroscopy (NRVS) measurements were performed on (57)Fe-labeled ferric Hydrogenobacter thermophilus cytochrome c-552, and variants M13V, M13V/K22M, and A7F, which have structural modifications that alter the composition or environment of the CXXCH pentapeptide loop. Simulations of the NRVS data indicate that the 150-325 cm(-1) region is dominated by NHis-Fe-SMet axial ligand and polypeptide motions, while the 325-400 cm(-1) region shows dominant contributions from ν(Fe-NPyr) (Pyr = pyrrole) and other heme-based modes. Diagnostic spectral signatures that directly relate to structural features of the heme active site are identified using a quantum chemistry-centered normal coordinate analysis (QCC-NCA). In particular, spectral features that directly correlate with CXXCH loop stiffness, the strength of the Fe-His interaction, and the degree of heme distortion are identified. Cumulative results from our investigation suggest that compared to the wild type (wt), variants M13V and M13V/K22M have a more rigid CXXCH pentapeptide segment, a stronger Fe-NHis interaction, and a more ruffled heme. Conversely, the A7F variant has a more planar heme and a weaker Fe-NHis bond. These results are correlated to the observed changes in reduction potential between wt protein and the variants studied here. Implications of these results for Cyt c biogenesis and electron transfer are also discussed.

The diagnostic vibrational signature of pentacoordination in heme carbonyls.

Heme-carbonyl complexes are widely exploited for the insight they provide into the structural basis of function in heme-based proteins, by revealing the nature of their bonded and nonbonded interactions with the protein. This report presents two novel results which clearly establish a FeCO vibrational signature for crystallographically verified pentacoordination. First, anisotropy in the NRVS density of states for ν(Fe-C) and δ(FeCO) in oriented single crystals of [Fe(OEP)(CO)] clearly reveals that the Fe-C stretch occurs at higher frequency than the FeCO bend and considerably higher than any previously reported heme carbonyl. Second, DFT calculations on a series of heme carbonyls reveal that the frequency crossover occurs near the weak trans O atom donor, furan. As ν(Fe-C) occurs at lower frequencies than δ(FeCO) in all heme protein carbonyls reported to date, the results reported herein suggest that they are all hexacoordinate.

Effects of imidazole deprotonation on vibrational spectra of high-spin iron(II) porphyrinates.

The effects of the deprotonation of coordinated imidazole on the vibrational dynamics of five-coordinate high-spin iron(II) porphyrinates have been investigated using nuclear resonance vibrational spectroscopy. Two complexes have been studied in detail with both powder and oriented single-crystal measurements. Changes in the vibrational spectra are clearly related to structural differences in the molecular structures that occur when imidazole is deprotonated. Most modes involving the simultaneous motion of iron and imidazolate are unresolved, but the one mode that is resolved is found at higher frequency in the imidazolates. These out-of-plane results are in accord with earlier resonance Raman studies of heme proteins. We also show the imidazole vs imidazolate differences in the in-plane vibrations that are not accessible to resonance Raman studies. The in-plane vibrations are at lower frequency in the imidazolate derivatives; the doming mode shifts are inconclusive. The stiffness, an experimentally determined force constant that averages the vibrational details to quantify the nearest-neighbor interactions, confirms that deprotonation inverts the relative strengths of axial and equatorial coordination.

Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals.

We have applied 57Fe nuclear resonance vibrational spectroscopy (NRVS) for the first time to study the dynamics of Fe centers in Fe-S protein crystals, including oxidized wild type rubredoxin crystals from Pyrococcus furiosus, and the MoFe protein of nitrogenase from Azotobacter vinelandii. Thanks to the NRVS selection rule, selectively probed vibrational modes have been observed in both oriented rubredoxin and MoFe protein crystals. The NRVS work was complemented by extended X-ray absorption fine structure spectroscopy (EXAFS) measurements on oxidized wild type rubredoxin crystals from Pyrococcus furiosus. The EXAFS spectra revealed the Fe-S bond length difference in oxidized Pf Rd protein, which is qualitatively consistent with the X-ray crystal structure.

Vibrational probes and determinants of the S = 0 ⇌ S = 2 spin crossover in five-coordinate [Fe(TPP)(CN)]-.

The low-frequency vibrational characterization of the spin-crossover complex, five-coordinate cyano(tetraphenylporphyrinato)iron(II), [Fe(TPP)(CN)](-), is reported. Nuclear resonance vibrational spectroscopy has been used to measure all low-frequency vibrations involving iron at several temperatures; this yields vibrational spectra of both the low- (S = 0) and high-spin (S = 2) states. Multitemperature oriented single-crystal measurements facilitate assignments of the vibrational character of all modes and are consistent with the DFT-predicted spectra. The availability of the entire iron vibrational spectrum allows for the complete correlation of the modes between the two spin states. These data demonstrate that not only do the frequencies of the vibrations shift to lower values for the high-spin species as would be expected owing to the weaker bonds in the high-spin state, but also the mixing of iron modes with ligand modes changes substantially. Diagrams illustrating the changing character of the modes and their correlation are given. The reduced iron-ligand frequencies are the primary factor in the entropic stabilization of the high-spin state responsible for the spin crossover.

Vibrational dynamics of oxygenated heme proteins.

Advanced spectroscopic techniques coupled with DFT calculations reveal the vibrational dynamics of the iron in stable dioxygen complexes with myoglobin and with a mutant engineered to model the catalytic site of heme-copper oxidases. The unprecedented level of detail will constrain computational modelling of reactions with oxygen.

Nuclear resonance vibrational spectra of five-coordinate imidazole-ligated iron(II) porphyrinates.

Nuclear resonance vibrational spectra have been obtained for six five-coordinate imidazole-ligated iron(II) porphyrinates, [Fe(Por)(L)] (Por = tetraphenylporphyrinate, octaethylporphyrinate, tetratolylporphyrinate, or protoporphyrinate IX and L = 2-methylimidazole or 1,2-dimethylimidazole). Measurements have been made on both powder and oriented crystal samples. The spectra are dominated by strong signals around 200-300 cm(-1). Although the in-plane and out-of-plane vibrations are seriously overlapped, oriented crystal spectra allow their deconvolution. Thus, oriented crystal experimental data, along with density functional theory (DFT) calculations, enable the assignment of key vibrations in the spectra. Molecular dynamics are also discussed. The nature of the Fe-N(Im) vibrations has been elaborated further than was possible from resonance Raman studies. Our study suggests that the Fe motions are coupled with the porphyrin core and peripheral groups motions. Both peripheral groups and their conformations have significant influence on the vibrational spectra (position and shape).

New perspectives on iron-ligand vibrations of oxyheme complexes.

We report our studies of the vibrational dynamics of iron for three imidazole-ligated oxyheme derivatives that mimic the active sites of histidine-ligated heme proteins complexed with dioxygen. The experimental vibrational data are obtained from nuclear resonance vibrational spectroscopy (NRVS) measurements conducted on both powder samples and oriented single crystals, and which includes several in-plane (ip) and out-of-plane (oop) measurements. Vibrational spectral assignments have been made through a combination of the oriented sample spectra and predictions based on density functional theory (DFT) calculations. The two Fe-O(2) modes that have been previously observed by resonance Raman spectroscopy in heme proteins are clearly shown to be very strongly mixed and are not simply either a bending or stretching mode. In addition, a third Fe-O(2) mode, not previously reported, has been identified. The long-sought Fe-Im stretch, not observed in resonance Raman spectra, has been identified and compared with the frequencies observed for the analogous CO and NO species. The studies also suggest that the in-plane iron motion is anisotropic and is controlled by the orientation of the Fe-O(2) group and not sensitive to the in-plane Fe-N(p) bonds and/or imidazole orientations.

Spectroscopic identification of reactive porphyrin motions.

Nuclear resonance vibrational spectroscopy (NRVS) reveals the vibrational dynamics of a Mössbauer probe nucleus. Here, (57)Fe NRVS measurements yield the complete spectrum of Fe vibrations in halide complexes of iron porphyrins. Iron porphine serves as a useful symmetric model for the more complex spectrum of asymmetric heme molecules that contribute to numerous essential biological processes. Quantitative comparison with the vibrational density of states (VDOS) predicted for the Fe atom by density functional theory calculations unambiguously identifies the correct sextet ground state in each case. These experimentally authenticated calculations then provide detailed normal mode descriptions for each observed vibration. All Fe-ligand vibrations are clearly identified despite the high symmetry of the Fe environment. Low frequency molecular distortions and acoustic lattice modes also contribute to the experimental signal. Correlation matrices compare vibrations between different molecules and yield a detailed picture of how heme vibrations evolve in response to (a) halide binding and (b) asymmetric placement of porphyrin side chains. The side chains strongly influence the energetics of heme doming motions that control Fe reactivity, which are easily observed in the experimental signal.

Bulk modulus of a protein active-site mimic.

Flexibility is an important property of porphyrins, both natural and synthetic. We applied two synchrotron-based techniques, nuclear resonance vibrational spectroscopy and inelastic X-ray scattering, to quantify this property by measuring the bulk modulus of a protein active-site mimic [chloro(octaethylporphyrinato)iron(III)] and the resilience of the iron environment. Their values are 6.95 ± 0.24 GPa and 15.4 ± 0.5 N/m, respectively.

Oriented single-crystal nuclear resonance vibrational spectroscopy of [Fe(TPP)(MI)(NO)]: quantitative assessment of the trans effect of NO.

This paper presents oriented single-crystal Nuclear Resonance Vibrational Spectroscopy (NRVS) data for the six-coordinate (6C) ferrous heme-nitrosyl model complex [(57)Fe(TPP)(MI)(NO)] (1; TPP(2-) = tetraphenylporphyrin dianion; MI = 1-methylimidazole). The availability of these data enables for the first time the detailed simulation of the complete NRVS data, including the porphyrin-based vibrations, of a 6C ferrous heme-nitrosyl, using our quantum chemistry centered normal coordinate analysis (QCC-NCA). Importantly, the Fe-NO stretch is split by interaction with a porphyrin-based vibration into two features, observed at 437 and 472 cm(-1). The 437 cm(-1) feature is strongly out-of-plane (oop) polarized and shows a (15)N(18)O isotope shift of 8 cm(-1) and is therefore assigned to nu(Fe-NO). The admixture of Fe-N-O bending character is small. Main contributions to the Fe-N-O bend are observed in the 520-580 cm(-1) region, distributed over a number of in-plane (ip) polarized porphyrin-based vibrations. The main component, assigned to delta(ip)(Fe-N-O), is identified with the feature at 563 cm(-1). The Fe-N-O bend also shows strong mixing with the Fe-NO stretching internal coordinate, as evidenced by the oop NRVS intensity in the 520-580 cm(-1) region. Very accurate normal mode descriptions of nu(Fe-NO) and delta(ip)(Fe-N-O) have been obtained in this study. These results contradict previous interpretations of the vibrational spectra of 6C ferrous heme-nitrosyls where the higher energy feature at approximately 550 cm(-1) had usually been associated with nu(Fe-NO). Furthermore, these results provide key insight into NO binding to ferrous heme active sites in globins and other heme proteins, in particular with respect to (a) the effect of hydrogen bonding to the coordinated NO and (b) changes in heme dynamics upon NO coordination. [Fe(TPP)(MI)(NO)] constitutes an excellent model system for ferrous NO adducts of myoglobin (Mb) mutants where the distal histidine (His64) has been removed. Comparison to the reported vibrational data for wild-type (wt) Mb-NO then shows that the effect of H bonding to the coordinated NO is weak and mostly leads to a polarization of the pi/pi* orbitals of bound NO. In addition, the observation that delta(ip)(Fe-N-O) does not correlate well with nu(N-O) can be traced back to the very mixed nature of this mode. The Fe-N(imidazole) stretching frequency is observed at 149 cm(-1) in [Fe(TPP)(MI)(NO)], and spectral changes upon NO binding to five-coordinate ferrous heme active sites are discussed. The obtained high-quality force constants for the Fe-NO and N-O bonds of 2.57 and 11.55 mdyn/A can further be compared to those of corresponding 5C species, which allows for a quantitative analysis of the sigma trans interaction between the proximal imidazole (His) ligand and NO. This is key for the activation of the NO sensor soluble guanylate cyclase. Finally, DFT methods are calibrated against the experimentally determined vibrational properties of the Fe-N-O subunit in 1. DFT is in fact incapable of reproducing the vibrational energies and normal mode descriptions of the Fe-N-O unit well, and thus, DFT-based predictions of changes in vibrational properties upon heme modification or other perturbations of these 6C complexes have to be treated with caution.

Nuclear resonance vibrational spectroscopy applied to [Fe(OEP)(NO)]: the vibrational assignments of five-coordinate ferrous heme-nitrosyls and implications for electronic structure.

This study presents Nuclear Resonance Vibrational Spectroscopy (NRVS) data on the five-coordinate (5C) ferrous heme-nitrosyl complex [Fe(OEP)(NO)] (1, OEP(2-) = octaethylporphyrinato dianion) and the corresponding (15)N(18)O labeled complex. The obtained spectra identify two isotope sensitive features at 522 and 388 cm(-1), which shift to 508 and 381 cm(-1), respectively, upon isotope labeling. These features are assigned to the Fe-NO stretch nu(Fe-NO) and the in-plane Fe-N-O bending mode delta(ip)(Fe-N-O), the latter has been unambiguously assigned for the first time for 1. The obtained NRVS data were simulated using our quantum chemistry centered normal coordinate analysis (QCC-NCA). Since complex 1 can potentially exist in 12 different conformations involving the FeNO and peripheral ethyl orientations, extended density functional theory (DFT) calculations and QCC-NCA simulations were performed to determine how these conformations affect the NRVS properties of [Fe(OEP)NO]. These results show that the properties and force constants of the FeNO unit are hardly affected by the conformational changes involving the ethyl substituents. On the other hand, the NRVS-active porphyrin-based vibrations around 340-360, 300-320, and 250-270 cm(-1) are sensitive to the conformational changes. The spectroscopic changes observed in these regions are due to selective mechanical couplings of one component of E(u)-type (in ideal D(4h) symmetry) porphyrin-based vibrations with the in-plane Fe-N-O bending mode. This leads to the observed variations in Fe(OEP) core mode energies and NRVS intensities without affecting the properties of the FeNO unit. The QCC-NCA simulated NRVS spectra of 1 show excellent agreement with experiment, and indicate that conformer F is likely present in the samples of this complex investigated here. The observed porphyrin-based vibrations in the NRVS spectra of 1 are also assigned based on the QCC-NCA results. The obtained force constants of the Fe-NO and N-O bonds are 2.83-2.94 (based on the DFT functional applied) and about 12.15 mdyn/A, respectively. The electronic structures of 5C ferrous heme-nitrosyls in different model complexes are then analyzed, and variations in their properties based on different porphyrin substituents are explained. Finally, the shortcomings of different DFT functionals in describing the axial FeNO subunit in heme-nitrosyls are elucidated.

Protein elasticity probed with two synchrotron-based techniques.

Compressibility characterizes three interconnecting properties of a protein: dynamics, structure, and function. The compressibility values for the electron-carrying protein cytochrome c and for other proteins, as well, available in the literature vary considerably. Here, we apply two synchrotron-based techniques--nuclear resonance vibrational spectroscopy and inelastic x-ray scattering--to measure the adiabatic compressibility of this protein. This is the first report of the compressibility of any material measured with this method. Unlike the methods previously used, this novel approach probes the protein globally, at ambient pressure, does not require the separation of protein and solvent contributions to the total compressibility, and uses samples that contain the heme iron, as in the native state. We show, by comparing our results with molecular dynamics predictions, that the compressibility is almost independent of temperature. We discuss potential applications of this method to other materials beyond proteins.

Sound velocities of compressed Fe3C from simultaneous synchrotron X-ray diffraction and nuclear resonant scattering measurements.

The applications of nuclear resonant scattering in laser-heated diamond anvil cells have provided an important probe for the magnetic and vibrational properties of (57)Fe-bearing materials under high pressure and high temperature. Synchrotron X-ray diffraction is one of the most powerful tools for studying phase stability and equation of state over a wide range of pressure and temperature conditions. Recently an experimental capability has been developed for simultaneous nuclear resonant scattering and X-ray diffraction measurements using synchrotron radiation. Here the application of this method to determine the sound velocities of compressed Fe(3)C is shown. The X-ray diffraction measurements allow detection of microscale impurities, phase transitions and chemical reactions upon compression or heating. They also provide information on sample pressure, grain size distribution and unit cell volume. By combining the Debye velocity extracted from the nuclear resonant inelastic X-ray scattering measurements and the structure, density and elasticity data from the X-ray diffraction measurements simultaneously obtained, more accurate sound velocity data can be derived. Our results on few-crystal and powder samples indicate strong anisotropy in the sound velocities of Fe(3)C under ambient conditions.

Electronic and magnetic structures of the postperovskite-type Fe2O3 and implications for planetary magnetic records and deep interiors.

Recent studies have shown that high pressure (P) induces the metallization of the Fe(2+)-O bonding, the destruction of magnetic ordering in Fe, and the high-spin (HS) to low-spin (LS) transition of Fe in silicate and oxide phases at the deep planetary interiors. Hematite (Fe(2)O(3)) is an important magnetic carrier mineral for deciphering planetary magnetism and a proxy for Fe in the planetary interiors. Here, we present synchrotron Mössbauer spectroscopy and X-ray diffraction combined with ab initio calculations for Fe(2)O(3) revealing the destruction of magnetic ordering at the hematite --> Rh(2)O(3)-II type (RhII) transition at 70 GPa and 300 K, and then the revival of magnetic ordering at the RhII --> postperovskite (PPv) transition after laser heating at 73 GPa. At the latter transition, at least half of Fe(3+) ions transform from LS to HS and Fe(2)O(3) changes from a semiconductor to a metal. This result demonstrates that some magnetic carrier minerals may experience a complex sequence of magnetic ordering changes during impact rather than a monotonic demagnetization. Also local Fe enrichment at Earth's core-mantle boundary will lead to changes in the electronic structure and spin state of Fe in silicate PPv. If the ultra-low-velocity zones are composed of Fe-enriched silicate PPv and/or the basaltic materials are accumulated at the lowermost mantle, high electrical conductivity of these regions will play an important role for the electromagnetic coupling between the mantle and the core.

Vibrational dynamics of iron in cytochrome C.

Nuclear resonance vibrational spectroscopy (NRVS) and Raman spectroscopy on (54)Fe- and (57)Fe-enriched cytochrome c (cyt c) identify multiple bands involving vibrations of the heme Fe. Comparison with predictions from Fe isotope shifts reveals that 70% of the NRVS signal in the 300-450 cm(-1) frequency range corresponds to vibrations resolved in Soret-enhanced Raman spectra. This frequency range dominates the "stiffness", an effective force constant determined by the Fe vibrational density of states (VDOS), which measures the strength of nearest-neighbor interactions with Fe. The stiffness of the low-spin Fe environment in both oxidation states of cyt c significantly exceeds that for the high-spin Fe in deoxymyoglobin, where the 200-300 cm(-1) frequency range dominates the VDOS. This situation is reflected in the shorter Fe-ligand bond lengths in the former with respect to the latter. The longer Fe-S(Met80) in oxidized cyt c with respect to reduced cyt c leads to a decrease in the stiffness of the iron environment upon oxidation. Comparison with NRVS measurements allows us to assess assignments for vibrational modes resolved in this region of the heme Raman spectrum. We consider the possibility that the 372 cm(-1) band in reduced cyt c involves the Fe-S(Met80) bond.