Investigation of the superconducting gap structure in κ-(BEDT-TTF)2Cu(NCS)2 and κ-(BEDT-TTF)2Cu[N(CN)2]Br by means of thermal-conductivity measurements.

We report temperature-dependent thermal-conductivity, κ, measurements on the layered quasi-two-dimensional organic superconductors κ-(BEDT-TTF)2Cu(NCS)2 and κ-(BEDT-TTF)2Cu[N(CN)2]Br down to 160 mK. The results for κ-(BEDT-TTF)2Cu(NCS)2 may be consistent with a nodal superconducting (SC) gap structure as indicated by a non-negligible remnant linear contribution when [Formula: see text] is extrapolated to [Formula: see text]. For κ-(BEDT-TTF)2Cu[N(CN)2]Br, contrary to expectations, higher κ values are observed in the superconducting regime as compared to the normal, high-field state evidencing a dominant phonon contribution to κ in the superconducting state. The strong increase of κ in the normal state below T c for both samples indicates strong electron-phonon scattering. Our results highlight the need for thermal-conductivity measurements performed down to significantly lower temperatures to determine the symmetry of the SC gap.

Nuclear Magnetic Resonance Signature of the Spin-Nematic Phase in LiCuVO_{4} at High Magnetic Fields.

We report a ^{51}V nuclear magnetic resonance investigation of the frustrated spin-1/2 chain compound LiCuVO_{4}, performed in pulsed magnetic fields and focused on high-field phases up to 56 T. For the crystal orientations H∥c and H∥b, we find a narrow field region just below the magnetic saturation where the local magnetization remains uniform and homogeneous, while its value is field dependent. This behavior is the first microscopic signature of the spin-nematic state, breaking spin-rotation symmetry without generating any transverse dipolar order, and is consistent with theoretical predictions for the LiCuVO_{4} compound.

Entropy Evolution in the Magnetic Phases of Partially Frustrated CePdAl.

In the heavy-fermion metal CePdAl, long-range antiferromagnetic order coexists with geometric frustration of one-third of the Ce moments. At low temperatures, the Kondo effect tends to screen the frustrated moments. We use magnetic fields B to suppress the Kondo screening and study the magnetic phase diagram and the evolution of the entropy with B employing thermodynamic probes. We estimate the frustration by introducing a definition of the frustration parameter based on the enhanced entropy, a fundamental feature of frustrated systems. In the field range where the Kondo screening is suppressed, the liberated moments tend to maximize the magnetic entropy and strongly enhance the frustration. Based on our experiments, this field range may be a promising candidate to search for a quantum spin liquid.

Field-stepped broadband NMR in pulsed magnets and application to SrCu2(BO3)2 at 54T.

Pulsed magnets generate the highest magnetic fields as brief transients during which the observation of NMR is difficult, however, this is the only route to unique insight into material properties up to the regime of 100T. Here, it is shown how rather broad NMR spectra can be assembled in a pulsed magnet during a single field pulse by using the inherent time dependence of the field for the recording of field-stepped free induction decays that cover a broad frequency range. The technique is then applied to (11)B NMR of the spin-dimer system SrCu2(BO3)2, a magnetic insulator known to undergo a series of field-driven changes of the magnetic ground state. At peak fields of about 54T at the Dresden High Magnetic Field Laboratory, (11)B NMR spectra spanning a total of about 9MHz width are reconstructed. The results are in good accordance with a change from a high-temperature paramagnetic state to a low-temperature commensurate superstructure of field-induced spin-dimer triplets.

NMR shift and relaxation measurements in pulsed high-field magnets up to 58T.

Nuclear magnetic resonance (NMR) experiments at fields up to 58T in pulsed magnets at the Dresden High Magnetic Field Laboratory are reported. The challenge to resolve NMR shifts in these time-dependent fields is addressed for the first time, and it is shown that this can indeed be accomplished with high precision with an internal reference. As a result, signal averaging is possible during a single magnetic field pulse, but also for multiple pulses. Thus, even very weak signals can in principle be recorded and their shifts can be determined. In a second set of experiments, the measurement of nuclear relaxation is investigated. Using adiabatic inversion with the inherent time dependence of the magnetic field and small-angle inspection, it is shown that relaxation measurements are possible, as well. The shift experiments were performed with (27)Al NMR on a mixture of aluminum metal and a Linde type A zeolite. For the relaxation studies, (27)Al NMR and (69)Ga NMR on the metals aluminum and gallium were preformed, respectively.

Distinct high-T transitions in underdoped Ba(1-x)KxFe2As2.

In contrast with the simultaneous structural and magnetic first order phase transition T0 previously reported, our detailed investigation on an underdoped Ba(0.84)K(0.16)Fe2As2 single crystal unambiguously revealed that the transitions are not concomitant. The tetragonal (τ: I4/mmm)-orthorhombic (ϑ: Fmmm) structural transition occurs at T(S)≃110 K, followed by an adjacent long-range antiferromagnetic (AFM) transition at T(N)≃102 K. Hysteresis and coexistence of the τ and ϑ phases over a finite temperature range observed by NMR experiments confirm the first order character of the τ-ϑ transition and provide evidence that both T(S) and T(N) are strongly correlated. Our data also show that superconductivity develops in the ϑ phase below T(c)=20 K and coexists with AFM. This new observation, T(S)≠T(N), firmly establishes another similarity between the hole-doped BaFe2As2 and the electron-doped iron-arsenide superconductors.

Mercuric chloride-induced spin or ligation state changes in ferric or ferrous human cystathionine beta-synthase inhibit enzyme activity.

Cystathionine beta-synthase is a key heme and pyridoxal phosphate-dependent enzyme involved in homocysteine metabolism in humans. The role of the recently discovered heme in this protein remains an important open question. The axial ligands to the heme in both the ferrous and ferric states have been assigned as cysteine and histidine residues, respectively. In this study, we have examined the effect of ligation and spin state changes in the heme on the activity of the enzyme. Treatment of the ferric enzyme with HgCl2 results in the conversion of six-coordinate low-spin heme to five-coordinate high-spin heme and is paralleled by a loss of activity. In contrast, treatment of the ferrous enzyme with HgCl2 results in replacement of the cysteine ligand by an unidentified sixth ligand and retention of the six-coordinate state, and is also accompanied by loss of enzyme activity. Treatment of the five-coordinate HgCl2-treated enzyme with thiols, such as homocysteine, results in reversion to a six-coordinate state. Resonance Raman spectroscopy with 34S-labeled enzyme reveals the return of the endogenous thiol ligand under these conditions and rules out direct coordination by the thiolate of homocysteine to the heme.

Cognitive occupational hazards and psychopathology of the artist.

The author discusses creativity and mental health issues, with a focus on epidemiology, risk factors, and possible treatment and risk reduction. Disorders by type of artist are briefly addressed.

Resonance Raman studies of cytochrome c' support the binding of NO and CO to opposite sides of the heme: implications for ligand discrimination in heme-based sensors.

Resonance Raman (RR) studies have been conducted on Alcaligenes xylosoxidans cytochrome c', a mono-His ligated hemoprotein which reversibly binds NO and CO but not O(2). Recent crystallographic characterization of this protein has revealed the first example of a hemoprotein which can utilize both sides of its heme (distal and proximal) for binding exogenous ligands to its Fe center. The present RR investigation of the Fe coordination and heme pocket environments of ferrous, carbonyl, and nitrosyl forms of cytochrome c' in solution fully supports the structures determined by X-ray crystallography and offers insights into mechanisms of ligand discrimination in heme-based sensors. Ferrous cytochrome c' reacts with CO to form a six-coordinate heme-CO complex, whereas reaction with NO results in cleavage of the proximal linkage to give a five-coordinate heme-NO adduct, despite the relatively high stretching frequency (231 cm(-1)) of the ferrous Fe-N(His) bond. RR spectra of the six-coordinate CO adduct indicate that CO binds to the Fe in a nonpolar environment in line with its location in the hydrophobic distal heme pocket. On the other hand, RR data for the five-coordinate NO adduct suggest a positively polarized environment for the NO ligand, consistent with its binding close to Arg 124 on the opposite (proximal) side of the heme. Parallels between certain physicochemical properties of cytochrome c' and those of heme-based sensor proteins raise the possibility that the latter may also utilize both sides of their hemes to discriminate between NO and CO binding.

Oral health status of second grade school children in upstate New York.

This report summarizes the results of a survey of second grade children conducted in upstate New York. The survey was designed to monitor progress toward achieving Healthy People 2000 objectives and Maternal and Child Health Services Block Grant performance measures. Data on oral health status, use of preventive measures and insurance coverage were collected on 2,474 children from 76 schools. In addition to obtaining population estimates, disparities in oral health between poor and nonpoor children were assessed. The results showed that approximately 52% of second grade children had dental caries, and 35% had untreated disease. Approximately 43% received fluoridated water, and 44% of children living in non-fluoridated areas used fluoride supplements on a regular basis. Only 25% of the children had dental sealants. The percentage of children covered by comprehensive and basic insurance plans was approximately 19% and 41%, respectively. Many of the national oral health objectives were not met primarily because of the higher rate of disease among the poor and their lower use of preventive services. These findings regarding oral health status and use of preventive services are similar to the national data.

Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme.

Human cystathionine beta-synthase (CBS) is an essential enzyme for the removal of the toxic metabolite homocysteine. Heme and pyridoxal phosphate (PLP) cofactors are necessary to catalyze the condensation of homocysteine and serine to generate cystathionine. While the role for the PLP cofactor is thought to be similar to that in other PLP-dependent enzymes that catalyze beta-replacement reactions, the exact role for the heme remains unclear. In this study, we have characterized the heme cofactor of CBS in both the ferric and ferrous states using resonance Raman spectroscopy. Positive identification of a cysteine ligand was achieved by global (34)S isotopic substitution which allowed us to assign the nu(Fe-S) for the six-coordinate low-spin ferric heme at 312 cm(-1). In addition, the CO adduct of ferrous CBS has vibrational frequencies characteristic of a histidine-heme-CO complex in a hydrophobic environment, and indicates that the Fe-S(Cys) bond is labile. We have also found that addition of HgCl(2) to the ferric heme causes conversion of the low-spin heme to a five-coordinate high-spin heme with loss of the cysteine ligand. The present spectroscopic studies do not support a reaction mechanism in which homocysteine binds directly to the heme via displacement of the Cys ligand in the binary enzyme complex, as had been previously proposed.

Reassessment of the active site quino-cofactor proposed to occur in the Aspergillus niger amine oxidase AO-I from the properties of model compounds.

Quino-cofactors have been found in a wide variety of prokaryotic and eukaryotic organisms. Two variants have, thus far, been demonstrated to derive from tyrosine precursors: these are the 2,4, 5-trihydroxyphenylalanine quinone (topa quinone or TPQ) [Janes, S. M. , et al. (1990) Science 248, 98] and an o-quinone analogue containing the side chain of a lysine residue (lysyltyrosine quinone or LTQ) [Wang, S. Z., et al. (1996) Science 273, 1078]. Additionally, a third variant of the family of tyrosine-derived cofactors has been reported to exist in an Aspergillus niger amine oxidase AO-I. This was described as an o-quinone cross-linked to the side chain of a glutamate residue [Frebort, I. (1996) Biochim. Biophys. Acta 1295, 59]. We have synthesized model compounds related to the proposed structure. Characterization of the redox properties for the model compound and spectral properties of its 4-nitrophenylhydrazine derivative lead us to conclude that the cofactor in A. niger amine oxidase AO-I has been misidentified. A TPQ carboxylate ester is considered an unlikely candidate for a biologically functional quino-cofactor.

Dean's fluorosis index: an assessment of examiner reliability.

OBJECTIVES: This report describes the interexaminer reliability achieved using Dean's Index in a study of dental fluorosis, and shows the effect on kappa values of assigning different weights to the various components of Dean's Index. METHODS: Three dentists conducted replicate fluorosis examinations on 202 children in Newburgh and Kingston, NY. Examiner reliability was assessed by computing percent agreement and weighted and unweighted kappa statistics. RESULTS: Agreement on the presence or absence of fluorosis using Dean's definition of fluorosis ranged from 92 to 97 percent and the respective kappa values ranged from 0.75 to 0.94. A comparison of subject-level severity scores for Dean's Index resulted in percent agreement ranging from 79.6 percent to 86.8 percent and kappa values ranging from 0.67 to 0.76. Weighting the kappa statistics improved agreement and reduced the differences. CONCLUSIONS: Examiners showed good to excellent agreement beyond chance in the use of the index. Subject level kappa scores were higher than tooth-level scores.

An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha.

The role of the active site aspartate base in the aminotransferase mechanism of the copper amine oxidase from the yeast Hansenula polymorpha has been probed by site-directed mutagenesis. The D319E mutant catalyzes the oxidation of methylamine and phenethylamine, but not that of benzylamine. kcat/Km for methylamine is found to be 80-fold reduced compared to that of the wild type. Viscosogen and substrate and solvent deuteration have no effect on this parameter for D319E, which is suggestive of limitation of kcat/Km by a conformational change. This conformational change is proposed to be the movement of the cofactor into a productive orientation upon the binding of substrate. In the absence of substrate, a flipped cofactor orientation is likely, on the basis of resonance Raman evidence that the C5 carbonyl of the cofactor is less solvent accessible than the C3 hydrogen. kcat for D319E methylamine oxidase is reduced 200-fold compared to that of the wild type and is unaffected by substrate deuteration, but displays a substantial solvent isotope effect. A 428 nm absorbance is evident under conditions of saturating methylamine and oxygen with D319E. The D319N mutant is observed to produce a similar absorbance at 430 nm when treated with ammonia despite the fact that this mutant has no amine oxidase activity. Resonance Raman spectroscopy indicates the formation of a covalent ammonia adduct and identifies it as the deprotonated iminoquinone. In contrast, when the D319E mutant is reacted with ammonia, it gives predominantly a 340-350 nm species. This absorbance is ascribed to a localization of the cofactor oxyanion induced by binding of the cation at the active site and not to covalent adduct formation. Resonance Raman spectroscopic examination of the steady state species of D319E methylamine oxidation, in combination with the kinetic data, indicates that the 428 nm species is the deprotonated iminoquinone produced upon reoxidation of the reduced cofactor. A model is proposed in which a central role of the active site base is to position the free cofactor and several enzyme intermediates for optimal activity.

Changes in dental fluorosis and dental caries in Newburgh and Kingston, New York.

OBJECTIVES: This study sought to determine whether the prevalence of dental fluorosis and dental caries had changed in a fluoridated community and a nonfluoridated community since an earlier study conducted in 1986. METHODS: Dental fluorosis and dental caries data were collected on 7- to 14-year-old lifelong residents (n = 1493) of Newburgh and Kingston, NY. RESULTS: Estimated dental fluorosis prevalence rates were 19.6% in Newburgh and 11.7% in Kingston. The greatest disparity in caries scores was observed between poor and nonpoor children in nonfluoridated Kingston. CONCLUSIONS: The prevalence of dental fluorosis has not declined in Newburgh and Kingston, whereas the prevalence of dental caries has continued to decline.

Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase from yeast.

A highly conserved asparagine residue is contained in the consensus site sequences of all known copper-containing amine oxidases (CAOs). On the basis of published crystallographic structures, the asparagine is found to reside proximal to the active site redox cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ). In this study, the conserved asparagine was changed to an alanine in a CAO from Hansenula polymorpha expressed in Saccharomyces cerevisiae, and the mutant's catalytic properties were characterized using steady-state kinetics and resonance Raman spectroscopy. Several lines of evidence point to TPQ exisiting in an nonproductive orientation in the mutant, including reductions in several steady-state parameters and an accumulation of an inactive product Schiff base complex when the enzyme is incubated with methylamine as the substrate. This product Schiff base complex was previously found to form following mutation of another conserved consensus site residue, a glutamate (or aspartate) at the C + 1 position from TPQ [Cai, D., Dove, J., Nakamura, N., Sanders-Loehr, J., and Klinman, J. P. (1997) Biochemistry 36, 11472-11478]. The results suggest that these two residues are crucial in maintaining the balance of cofactor mobility versus rigidity expected to be necessary during the dual processes of biogenesis and catalysis, respectively, that all CAOs must accomplish. In addition, a previously unidentified structural linkage between these two highly conserved residues is proposed which spans both subunits of the dimeric CAOs, and may have implications for intersubunit communication.

Recommendations for fluoride use in children. A review.

Fluoride has played a significant role in the improvement of the oral health of all Americans. Because of its effectiveness, cost and frequency of exposure, water fluoridation is the preferred method of delivery. Today, many products containing fluoride are available over the counter and as prescription items. The potential for exposure to multiple sources of fluoride has increased. Therefore, practitioners should prescribe fluoride therapy based on an understanding of patients' total exposure to fluoride and the need for additional amounts.

The complex between retinol and retinol-binding protein is formed in the rough microsomes of liver following repletion of vitamin A-depleted rats.

Retinol-binding protein (RBP), the plasma transport protein for vitamin A, is primarily synthesized in the rough endoplasmic reticulum of the liver. RBP then passes through the smooth endoplasmic reticulum and into the Golgi apparatus where vesicles form and transport the protein to the cell membrane. When rats were depleted of their vitamin A stores, RBP accumulated in the liver microsomes, particularly in the rough microsomes. To identify the organelle(s) where retinol initially binds to RBP, vitamin A-depleted rats were given an i.v. injection of [3H]retinol suspended in Tween 40. After intervals of 2, 3, 4, 5, 6, 8, 10, 15 and 20 min, liver fractions enriched in rough and smooth microsomes and Golgi apparatus were prepared. The retinol/RBP complex (holoRBP) was detected in the rough microsomes within 3 min post injection. HoloRBP later appeared in the smooth microsomes and Golgi fraction, and then the serum at time intervals consistent with the known secretion rate for RBP. HoloRBP was detected in the rough microsomes at all times after 3 min, whether or not the complex was present in the other subcellular fractions. Thus, the holoRBP complex can form in the rough endoplasmic reticulum of the liver.

Evaluation of a school-based sealant program in New York State.

This study evaluated the outcome of a targeted dental sealant program by comparing the survival probabilities of sealed high-risk first molar tooth sites to unsealed low-risk tooth sites in 1,122 children enrolled in a school-based sealant program. A comparison of the survival probabilities between low-risk first molar teeth that did not receive sealants and the sealed high-risk first molar teeth did not show significant differences. The results suggest that the protocol used by the program provides a satisfactory method for identification of children who could best benefit from sealants in a school-based situation.