Observation of universal Hall response in strongly interacting Fermions.

The Hall effect, which originates from the motion of charged particles in magnetic fields, has deep consequences for the description of materials, extending far beyond condensed matter. Understanding such an effect in interacting systems represents a fundamental challenge, even for small magnetic fields. In this work, we used an atomic quantum simulator in which we tracked the motion of ultracold fermions in two-leg ribbons threaded by artificial magnetic fields. Through controllable quench dynamics, we measured the Hall response for a range of synthetic tunneling and atomic interaction strengths. We unveil a universal interaction-independent behavior above an interaction threshold, in agreement with theoretical analyses. The ability to reach hard-to-compute regimes demonstrates the power of quantum simulation to describe strongly correlated topological states of matter.

Hidden Order and Symmetry Protected Topological States in Quantum Link Ladders.

We show that, whereas spin-1/2 one-dimensional U(1) quantum-link models (QLMs) are topologically trivial, when implemented in ladderlike lattices these models may present an intriguing ground-state phase diagram, which includes a symmetry protected topological (SPT) phase that may be readily revealed by analyzing long-range string spin correlations along the ladder legs. We propose a simple scheme for the realization of spin-1/2 U(1) QLMs based on single-component fermions loaded in an optical lattice with s and p bands, showing that the SPT phase may be experimentally realized by adiabatic preparation.

Vortex-Hole Duality: A Unified Picture of Weak- and Strong-Coupling Regimes of Bosonic Ladders with Flux.

Two-leg bosonic ladders with flux harbor a remarkable vortex-hole duality between the weak-coupling vortex lattice superfluids and strong-coupling charge-density-wave crystals. The strong-coupling crystalline states, which are realized in the vicinity of π flux, are independent of particle statistics, and are related to the incompressible fractional quantum Hall states in the thin-cylinder limit. These fully gapped ground states, away from π flux, develop nonzero chiral (spin) currents. Contact-interacting quantum gases permit exploration of this vortex-hole duality in experiments.

Spontaneous Increase of Magnetic Flux and Chiral-Current Reversal in Bosonic Ladders: Swimming against the Tide.

The interplay between spontaneous symmetry breaking in many-body systems, the wavelike nature of quantum particles and lattice effects produces an extraordinary behavior of the chiral current of bosonic particles in the presence of a uniform magnetic flux defined on a two-leg ladder. While noninteracting as well as strongly interacting particles, stirred by the magnetic field, circulate along the system's boundary in the counterclockwise direction in the ground state, interactions stabilize vortex lattices. These states break translational symmetry, which can lead to a reversal of the circulation direction. Our predictions could readily be accessed in quantum gas experiments with existing setups or in arrays of Josephson junctions.

Density-dependent synthetic gauge fields using periodically modulated interactions.

We show that density-dependent synthetic gauge fields may be engineered by combining periodically modulated interactions and Raman-assisted hopping in spin-dependent optical lattices. These fields lead to a density-dependent shift of the momentum distribution, may induce superfluid-to-Mott insulator transitions, and strongly modify correlations in the superfluid regime. We show that the interplay between the created gauge field and the broken sublattice symmetry results, as well, in an intriguing behavior at vanishing interactions, characterized by the appearance of a fractional Mott insulator.

X-linked dyskeratosis congenita is predominantly caused by missense mutations in the DKC1 gene.

Dyskeratosis congenita is a rare inherited bone marrow-failure syndrome characterized by abnormal skin pigmentation, nail dystrophy, and mucosal leukoplakia. More than 80% of patients develop bone-marrow failure, and this is the major cause of premature death. The X-linked form of the disease (MIM 305000) has been shown to be caused by mutations in the DKC1 gene. The gene encodes a 514-amino-acid protein, dyskerin, that is homologous to Saccharomyces cerevisiae Cbf5p and rat Nap57 proteins. By analogy to the homologues in other species, dyskerin is predicted to be a nucleolar protein with a role in both the biogenesis of ribosomes and, in particular, the pseudouridylation of rRNA precursors. We have determined the genomic structure of the DKC1 gene; it consists of 15 exons spanning a region of 15 kb. This has enabled us to screen for mutations in the genomic DNA, by using SSCP analysis. Mutations were detected in 21 of 37 additional families with dyskeratosis congenita that were analyzed. These mutations consisted of 11 different single-nucleotide substitutions, which resulted in 10 missense mutations and 1 putative splicing mutation within an intron. The missense change A353V was observed in 10 different families and was shown to be a recurring de novo event. Two polymorphisms were also detected, one of which resulted in the insertion of an additional lysine in the carboxy-terminal polylysine domain. It is apparent that X-linked dyskeratosis congenita is predominantly caused by missense mutations; the precise effect on the function of dyskerin remains to be determined.

Substrate induced changes of the active site electronic states in reduced cytochrome P450cam and the photolysis product of its CO complex. Low-temperature magnetic circular dichroism data.

MCD spectra of camphor-free and camphor-bound reduced cytochrome P450cam have been recorded for the near UV and visible spectral regions at temperatures from 300K down to 2.1K and compared with those of the carbon monoxide photoproducts generated at 4.2K. In the absence of camphor, the reduced P450 is spectroscopically different from the photoproduct. In the presence of camphor, however, the spectra of the reduced P450 and of the photoproduct are almost similar and behave like the photoproduct of the camphor-free enzyme. This behavior indicates that substrate binding induces a higher active site rigidity. From the significant alteration of the temperature dependence of the MCD intensity for the reduced enzyme induced by camphor binding it is concluded that the near degeneracy of the electronic ground state in the substrate-free enzyme is removed by substrate binding.

Low- and ultralow-temperature magnetic circular dichroism studies of reduced cytochromes P-450-LM2 and P-420-LM2 and of photo-products of their co-complexes. The spin-state and axial ligation of heme iron.

MCD spectra of reduced cytochromes P-450 and P-420 have been recorded in the spectral region 350-800 nm at temperatures 4.2-290 K and were compared with the respective low-temperature photolysed CO-complexes at 4.2 K. The MCD data are consistent with the suggestions that: the heme iron is high-spin in the reduced proteins and in the photolysed species; mercaptide is the protein-derived ligand of the heme iron in the reduced cytochrome P-450, as well as in its CO-complex; imidazole of histidine is the fifth ligand of the heme iron both in the reduced P-420 and its CO-complex; structural changes in the heme iron coordination sphere occur at CO-binding.

[Comparison of the heme electron state of reduced cytochrome P450 and P420 in equilibrium and non-equilibrium protein conformations. The nature of the protein heme ligand]. / Sravnenie élektronnykh sostoianii gema vosstanovlennykh tsitokhromov P450 i P420 v ravnovesnoi i neravnovesnoi konformatsii belka. Priroda belkovogo liganda gema.

Magnetic circular dichroism (MCD) spectra of reduced cytochromes P450 and P420 in equilibrium and non-equilibrium protein conformations are compared at 4.2 K for the 350-800 spectral region. Non-equilibrium forms have been produced by photolysis of CO-complexes at 4.2 K. The differences between MCD spectra of proteins in equilibrium and non-equilibrium conformations, in particular for the visible region, show clearly the structural changes in the heme iron coordination sphere to occur on ligand binding. The comparison of the Soret MCD spectra of reduced proteins in their equilibrium and non-equilibrium forms with those of other high-spin ferrous hemoproteins suggest that mercaptide (RS-) is the protein ligand of the heme iron in reduced P450, as well as in its CO-complex, and that imidazole of histidine is the fifth ligand of the iron both in reduced P420 and its CO-complex. The thermal recombination of the photoproducts with CO have been studied. When temperature rises from 4.2 to 77 K for two hours both proteins have similar temperature characteristics during the recombination processes. The recombination begins at T approximately equal to 10 K and is completed at approximately equal to 50 K. The temperature at which half of the total photolyzed molecules are restored to the CO-form is equal to 25 K. For products of photolysis of CO-complexes of myoglobin and hemoglobin under the same heating conditions these temperatures are equal to 35 and 23 K respectively. Thus, the photoproducts of P450, P420 and hemoglobin have similar parameters of low-temperature recombination and the kinetics of this process is faster than for photodissociated myoglobin.

Kinetics of elementary steps in the cytochrome P-450 reaction sequence. V. Laser temperature-jump investigation of the spin relaxation kinetics of cytochrome P-450 LM2.

The cytochrome P-450 LM2 spin state relaxation kinetics has been resolved by means of laser temperature-jump techniques. The first order rate constants amount to about 10(6) S-1 in the substrate-free and the substrate-bound protein, respectively. Evidence is provided that the spin equilibrium preequilibrates the P-450 reduction but is not rate-limiting. Additional capacitor discharge temperature-jump studies elucidate substrate dependent perturbations.

Absorption spectra of highly purified liver microsomal cytochrome P-450 in non-equilibrium conformational states at low temperatures.

Absorption spectra of highly purified liver microsomal cytochrome P-450 in non-equilibrium states were obtained at 77 K by reduction with trapped electrons, formed by gamma-irradiation of the water-glycerol matrix. In contrast to the equilibrium form of ferrous cytochrome P-450 with the heme iron in the high-spin state the non-equilibrium ferrous state has a low-spin heme iron. The absorption spectrum of the non-equilibrium ferrous cytochrome P-450 is characterized by two bands at 564 (alpha-band) and 530 nm (beta-band). When the temperature is increased to about 278 K this non-equilibrium form of the reduced enzyme is relaxed to the corresponding equilibrium form with a single absorption band at 548 nm in the visible region characteristic for a high-spin heme iron.

Quantitative analysis of the spin equilibrium of cytochrome P-450 LM2 fraction from rabbit liver microsomes.

The LM2 fraction of cytochrome P-450 from phenobarbital induced rabbit liver microsomes in the presence and in the absence of substrate (benzphetamine) is shown to be a thermal equilibrium of a high spin (S = 5/2) and a low spin (S = 1/2) state each of which exhibiting its individual optical basic spectrum with the Soret maxima at 387 nm and 417 nm for the high spin form and the low spin form, respectively. The equilibrium constants and thermodynamic parameters describing the spin transition and the substrate binding have been evaluated from the temperature and substrate difference spectra. These two interacting equilibria are presented in terms of a thermodynamic model, which provides a quantitative description of the relationship between the substrate binding and the spin equilibrium. From kinetic experiments it is concluded that the spin equilibrium is an electronic one and is not caused by iron ligand dissociation.

Spectral properties of nonequilibrium states in cytochrome P-450 formed by reduction at subzero temperatures.

Nonequilibrium conformational states in cytochrome P-450 in the presence and absence of substrates formed by reduction at subzero temperatures with hydrates electrons were obtained and characterized by their absorption spectra. Different absorption spectra between the relaxed (298 K) and the non-relaxed enzyme forms (77 K) indicate conformational changes proceeding in the relaxed form after reduction of the heme iron which lead to altered interactions between the active centre and its environment in the protein. The two maxima of the nonequilibrium form of cytochrome P-450 without substrate in the visible absorption spectrum (alpha-band, beta-band) and the ratio of their intensities indicate the low-spin character of the heme iron. These spectral properties give evidence for a reduced cytochrome P-450 with two heme-linked axial ligands.