ABSTRACT
Many-body localization (MBL) has attracted significant attention because of its immunity to thermalization, role in logarithmic entanglement entropy growth, and opportunities to reach exotic quantum orders. However, experimental realization of MBL in solid-state systems has remained challenging. Here, we report evidence of a possible phonon MBL phase in disordered GaAs/AlAs superlattices. Through grazing-incidence inelastic X-ray scattering, we observe a strong deviation of the phonon population from equilibrium in samples doped with ErAs nanodots at low temperature, signaling a departure from thermalization. This behavior occurs within finite phonon energy and wavevector windows, suggesting a localization-thermalization crossover. We support our observation by proposing a theoretical model for the effective phonon Hamiltonian in disordered superlattices, and showing that it can be mapped exactly to a disordered 1D Bose-Hubbard model with a known MBL phase. Our work provides momentum-resolved experimental evidence of phonon localization, extending the scope of MBL to disordered solid-state systems.
Subject(s)
Models, Theoretical , PhononsABSTRACT
Inelastic X-ray scattering is a powerful and versatile technique for studying lattice dynamics in materials of scientific and technological importance. In this article, the design and capabilities of the momentum-resolved high-energy-resolution inelastic X-ray spectrometer (HERIX) at beamline 30-ID of the Advanced Photon Source are reported. The instrument operates at 23.724â keV and has an energy resolution of 1.3-1.7â meV. It can accommodate momentum transfers of up to 72â â nm-1, at a typical X-ray flux of 4.5â ×â 109â photons s-1 meV-1 at the sample. A suite of inâ situ sample environments are provided, including high pressure, static magnetic fields and uniaxial strains, all at high or cryogenic temperatures.
ABSTRACT
Phase competition underlies many remarkable and technologically important phenomena in transition metal oxides. Vanadium dioxide (VO2) exhibits a first-order metal-insulator transition (MIT) near room temperature, where conductivity is suppressed and the lattice changes from tetragonal to monoclinic on cooling. Ongoing attempts to explain this coupled structural and electronic transition begin with two alternative starting points: a Peierls MIT driven by instabilities in electron-lattice dynamics and a Mott MIT where strong electron-electron correlations drive charge localization. A key missing piece of the VO2 puzzle is the role of lattice vibrations. Moreover, a comprehensive thermodynamic treatment must integrate both entropic and energetic aspects of the transition. Here we report that the entropy driving the MIT in VO2 is dominated by strongly anharmonic phonons rather than electronic contributions, and provide a direct determination of phonon dispersions. Our ab initio calculations identify softer bonding in the tetragonal phase, relative to the monoclinic phase, as the origin of the large vibrational entropy stabilizing the metallic rutile phase. They further reveal how a balance between higher entropy in the metal and orbital-driven lower energy in the insulator fully describes the thermodynamic forces controlling the MIT. Our study illustrates the critical role of anharmonic lattice dynamics in metal oxide phase competition, and provides guidance for the predictive design of new materials.
ABSTRACT
Material properties depend sensitively on the atomic arrangements and atomic bonding, but these are notoriously difficult to measure in nanosized atomic clusters due to the small size of the objects and the challenge of obtaining bulk samples of identical clusters. Here, we have combined the recent ability to make gram quantities of identical semiconductor quantum-dot nanoparticles with the ability to measure lattice dynamics on small sample quantities of hydrogenated materials using high energy resolution inelastic x-ray scattering, to measure the size dependence of the phonon density of states in CdSe quantum dots. The fact that we have atomically precise structural models for these nanoparticles allows the calculation of the phonon density of states using density functional theory, providing both experimental and theoretical confirmations of the important role that the inertia of the surface capping species plays on determining the lattice dynamics.
ABSTRACT
We used a newer, synchrotron-based, spectroscopic technique (nuclear resonance vibrational spectroscopy, NRVS) in combination with a more traditional one (infrared absorption, IR) to obtain a complete, quantitative picture of the metal center vibrational dynamics in a six-coordinated tin porphyrin. From the NRVS (119)Sn site-selectivity and the sensitivity of the IR signal to (112)Sn/(119)Sn isotope substitution, we identified the frequency of the antisymmetric stretching of the axial bonds (290 cm(-1)) and all the other vibrations involving Sn. Experimentally authenticated density functional theory (DFT) calculations aid the data interpretation by providing detailed normal mode descriptions for each observed vibration. These results may represent a starting point toward the characterization of the local vibrational dynamics of the metallic site in tin porphyrins and compounds with related structures. The quantitative complementariness between IR, NRVS, and DFT is emphasized.
Subject(s)
Metalloporphyrins/chemistry , Tin/chemistry , Models, Molecular , Quantum Theory , Spectrophotometry, InfraredABSTRACT
Investigation of the heme iron dynamics in cytochrome c with Mössbauer spectroscopy and especially nuclear resonance vibrational spectroscopy requires the replacement of the natural abundant heme iron with the (57)Fe isotope. For demetallization, we use a safer and milder ferrous sulfate-hydrochloric acid method in addition to the harsher commonly used hydrofluoric acid-based procedure. The structural integrity of the (57)Fe-reconstituted protein in both oxidation states is confirmed from absorption spectra and a detailed analysis of the rich resonance Raman spectra. These results reinforce the application of metal-substituted heme c proteins as reliable models for the native proteins.
Subject(s)
Cytochromes c/chemistry , Spectroscopy, Mossbauer , Cytochromes c/metabolism , Ferrous Compounds/chemistry , Heme/chemistry , Hydrochloric Acid/chemistry , Iron Isotopes/chemistry , Models, Molecular , Oxidation-Reduction , Spectrum Analysis, Raman , VibrationABSTRACT
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.
Subject(s)
Cytochrome c Group/chemistry , Elasticity , Animals , Horses , Scattering, Radiation , Spectrum Analysis , X-RaysABSTRACT
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.
Subject(s)
Cytochromes c/chemistry , Iron/chemistry , Iron Isotopes , Models, Molecular , Nuclear Magnetic Resonance, Biomolecular , Spectrum Analysis, Raman , VibrationABSTRACT
Conformational flexibility is essential to the functional behavior of proteins. We use an effective force constant introduced by Zaccai, the resilience, to quantify this flexibility. Site-selective experimental and computational methods allow us to determine the resilience of heme protein active sites. The vibrational density of states of the heme Fe determined using nuclear resonance vibrational spectroscopy provides a direct experimental measure of the resilience of the Fe environment, which we compare quantitatively with values derived from the temperature dependence of atomic mean-squared displacements in molecular dynamics simulations. Vibrational normal modes in the THz frequency range dominate the resilience. Both experimental and computational methods find a higher resilience for cytochrome c than for myoglobin, which we attribute to the increased number of covalent links to the peptide in the former protein. For myoglobin, the resilience of the iron environment is larger than the average resilience previously determined for hydrogen sites using neutron scattering. Experimental results suggest a slightly reduced resilience for cytochrome c upon oxidation, although the change is smaller than reported in previous Mössbauer investigations on a bacterial cytochrome c, and is not reproduced by the simulations. Oxidation state also has no significant influence on the compressibility calculated for cyt c, although a slightly larger compressibility is predicted for myoglobin.
Subject(s)
Hemeproteins/chemistry , Hemeproteins/metabolism , Iron/chemistry , Iron/metabolism , Cytochromes c/chemistry , Cytochromes c/metabolism , Models, Molecular , Myoglobin/chemistry , Myoglobin/metabolism , Protein Conformation , Temperature , VibrationABSTRACT
The control of phonon propagation in nanoparticle arrays is one of the frontiers of nanotechnology, potentially enabling the discovery of materials with unknown functionalities for potential innovative applications. The exploration of the terahertz window appears quite promising as phonons in this range are the leading carriers of heat transport in insulators and their control is the key to implement devices for heat flow management. Unfortunately, this scientific field is still in its infancy, and even a basic topic such as the influence of floating nanoparticles on the terahertz phonon propagation of a colloidal suspension still eludes a firm answer. Shedding some light on this topic is the main motivation of the present work, which focuses an inelastic X-ray scattering (IXS) measurements on a dilute suspension of Au nanospheres in water. Measured spectra showed a nontrivial shape displaying multiple inelastic features that, based on a Bayesian inference analysis, we assign to phonon modes propagating throughout the nanoparticle interior. Surprisingly, the spectra bear no evidence of propagating modes, which are known to dominate the spectrum of pure water, owing to the scattering that these modes suffer from the sparse nanoparticles in suspension. In perspective, this finding may inspire simple routes to manipulate high-frequency acoustic propagation in hybrid-liquid and solid-materials.
ABSTRACT
High-resolution X-ray measurements near a nuclear resonance reveal the complete vibrational spectrum of the probe nucleus. Because of this, nuclear resonance vibrational spectroscopy (NRVS) is a uniquely quantitative probe of the vibrational dynamics of reactive iron sites in proteins and other complex molecules. Our measurements of vibrational fundamentals have revealed both frequencies and amplitudes of (57)Fe vibrations in proteins and model compounds. Information on the direction of Fe motion has also been obtained from measurements on oriented single crystals, and provides an essential test of normal mode predictions. Here, we report the observation of weaker two-quantum vibrational excitations (overtones and combinations) for compounds that mimic the active site of heme proteins. The predicted intensities depend strongly on the direction of Fe motion. We compare the observed features with predictions based on the observed fundamentals, using information on the direction of Fe motion obtained either from DFT predictions or from single crystal measurements. Two-quantum excitations may become a useful tool to identify the directions of the Fe oscillations when single crystals are not available.
ABSTRACT
Magnetite exhibits unique electronic, magnetic, and structural properties in extreme conditions that are of great research interest. Previous studies have suggested a number of transitional models, although the nature of magnetite at high pressure remains elusive. We have studied a highly stoichiometric magnetite using inelastic X-ray scattering, X-ray diffraction and emission, and Raman spectroscopies in diamond anvil cells up to ~20 GPa, while complementary electrical conductivity measurements were conducted in a cubic anvil cell up to 8.5 GPa. We have observed an elastic softening in the diagonal elastic constants (C11 and C44) and a hardening in the off-diagonal constant (C12) at ~8 GPa where significant elastic anisotropies in longitudinal and transverse acoustic waves occur, especially along the [110] direction. An additional vibrational Raman band between the A1g and T2g modes was also detected at the transition pressure. These abnormal elastic and vibrational behaviors of magnetite are attributed to the occurrence of the octahedrally-coordinated Fe(2+)-Fe(3+)-Fe(2+) ions charge-ordering along the [110] direction in the inverse spinel structure. We propose a new phase diagram of magnetite in which the temperature for the metal-insulator and distorted structural transitions decreases with increasing pressure while the charge-ordering transition occurs at ~8 GPa and room temperature.
ABSTRACT
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.
Subject(s)
Hemeproteins/chemistry , Porphyrins/chemistry , Animals , Biomimetics , Catalytic Domain , Humans , Models, Molecular , Spectrum AnalysisABSTRACT
We use nuclear resonance vibrational spectroscopy and computational predictions based on density functional theory (DFT) to explore the vibrational dynamics of (57)Fe in porphyrins that mimic the active sites of histidine-ligated heme proteins complexed with carbon monoxide. Nuclear resonance vibrational spectroscopy yields the complete vibrational spectrum of a Mössbauer isotope, and provides a valuable probe that is not only selective for protein active sites but quantifies the mean-squared amplitude and direction of the motion of the probe nucleus, in addition to vibrational frequencies. Quantitative comparison of the experimental results with DFT calculations provides a detailed, rigorous test of the vibrational predictions, which in turn provide a reliable description of the observed vibrational features. In addition to the well-studied stretching vibration of the Fe-CO bond, vibrations involving the Fe-imidazole bond, and the Fe-N(pyr) bonds to the pyrrole nitrogens of the porphyrin contribute prominently to the observed experimental signal. All of these frequencies show structural sensitivity to the corresponding bond lengths, but previous studies have failed to identify the latter vibrations, presumably because the coupling to the electronic excitation is too small in resonance Raman measurements. We also observe the FeCO bending vibrations, which are not Raman active for these unhindered model compounds. The observed Fe amplitude is strongly inconsistent with three-body oscillator descriptions of the FeCO fragment, but agrees quantitatively with DFT predictions. Over the past decade, quantum chemical calculations have suggested revised estimates of the importance of steric distortion of the bound CO in preventing poisoning of heme proteins by carbon monoxide. Quantitative agreement with the predicted frequency, amplitude, and direction of Fe motion for the FeCO bending vibrations provides direct experimental support for the quantum chemical description of the energetics of the FeCO unit.
Subject(s)
Iron/chemistry , Porphyrins/chemistry , Computational Biology , Magnetic Resonance Spectroscopy , Models, ChemicalABSTRACT
We use nuclear resonance vibrational spectroscopy (NRVS) to identify the Fe-NO stretching frequency in the NO adduct of myoglobin (MbNO) and in the related six-coordinate porphyrin Fe(TPP)(1-MeIm)(NO). Frequency shifts observed in MbNO Raman spectra upon isotopic substitution of Fe or the nitrosyl nitrogen confirm and extend the NRVS results. In contrast with previous assignments, the Fe-NO frequency of these six-coordinate complexes lies 70-100 cm-1 lower than in the analogous five-coordinate nitrosyl complexes, indicating a significant weakening of the Fe-NO bond in the presence of a trans imidazole ligand. This result supports proposed mechanisms for NO activation of heme proteins and underscores the value of NRVS as a direct probe of metal reactivity in complex biomolecules.
Subject(s)
Hemeproteins/chemistry , Iron/chemistry , Nitric Oxide/chemistry , Nuclear Magnetic Resonance, Biomolecular , VibrationABSTRACT
We use quantitative experimental and theoretical approaches to characterize the vibrational dynamics of the Fe atom in porphyrins designed to model heme protein active sites. Nuclear resonance vibrational spectroscopy (NRVS) yields frequencies, amplitudes, and directions for 57Fe vibrations in a series of ferrous nitrosyl porphyrins, which provide a benchmark for evaluation of quantum chemical vibrational calculations. Detailed normal mode predictions result from DFT calculations on ferrous nitrosyl tetraphenylporphyrin Fe(TPP)(NO), its cation [Fe(TPP)(NO)]+, and ferrous nitrosyl porphine Fe(P)(NO). Differing functionals lead to significant variability in the predicted Fe-NO bond length and frequency for Fe(TPP)(NO). Otherwise, quantitative comparison of calculated and measured Fe dynamics on an absolute scale reveals good overall agreement, suggesting that DFT calculations provide a reliable guide to the character of observed Fe vibrational modes. These include a series of modes involving Fe motion in the plane of the porphyrin, which are rarely identified using infrared and Raman spectroscopies. The NO binding geometry breaks the four-fold symmetry of the Fe environment, and the resulting frequency splittings of the in-plane modes predicted for Fe(TPP)(NO) agree with observations. In contrast to expectations of a simple three-body model, mode energy remains localized on the FeNO fragment for only two modes, an N-O stretch and a mode with mixed Fe-NO stretch and FeNO bend character. Bending of the FeNO unit also contributes to several of the in-plane modes, but no primary FeNO bending mode is identified for Fe(TPP)(NO). Vibrations associated with hindered rotation of the NO and heme doming are predicted at low frequencies, where Fe motion perpendicular to the heme is identified experimentally at 73 and 128 cm-1. Identification of the latter two modes is a crucial first step toward quantifying the reactive energetics of Fe porphyrins and heme proteins.