Nuclear and magnetic spin structure of the antiferromagnetic triangular lattice compound LiCrTe2 investigated by [Formula: see text]SR, neutron and X-ray diffraction.

Two-dimensional (2D) triangular lattice antiferromagnets (2D-TLA) often manifest intriguing physical and technological properties, due to the strong interplay between lattice geometry and electronic properties. The recently synthesized 2-dimensional transition metal dichalcogenide LiCrTe[Formula: see text], being a 2D-TLA, enriched the range of materials which can present such properties. In this work, muon spin rotation ([Formula: see text]SR) and neutron powder diffraction (NPD) have been utilized to reveal the true magnetic nature and ground state of LiCrTe[Formula: see text]. From high-resolution NPD the magnetic spin order at base-temperature is not, as previously suggested, helical, but rather collinear antiferromagnetic (AFM) with ferromagnetic (FM) spin coupling within the ab-plane and AFM coupling along the c-axis. The value if the ordered magnetic Cr moment is established as [Formula: see text]. From detailed [Formula: see text]SR measurements we observe an AFM ordering temperature [Formula: see text] K. This value is remarkably higher than the one previously reported by magnetic bulk measurements. From [Formula: see text]SR we are able to extract the magnetic order parameter, whose critical exponent allows us to categorize LiCrTe[Formula: see text] in the 3D Heisenberg AFM universality class. Finally, by combining our magnetic studies with high-resolution synchrotron X-ray diffraction (XRD), we find a clear coupling between the nuclear and magnetic spin lattices. This suggests the possibility for a strong magnon-phonon coupling, similar to what has been previously observed in the closely related compound LiCrO[Formula: see text].

Improving Model-Based Genetic Programming for Symbolic Regression of Small Expressions.

The Gene-pool Optimal Mixing Evolutionary Algorithm (GOMEA) is a model-based EA framework that has been shown to perform well in several domains, including Genetic Programming (GP). Differently from traditional EAs where variation acts blindly, GOMEA learns a model of interdependencies within the genotype, that is, the linkage, to estimate what patterns to propagate. In this article, we study the role of Linkage Learning (LL) performed by GOMEA in Symbolic Regression (SR). We show that the non-uniformity in the distribution of the genotype in GP populations negatively biases LL, and propose a method to correct for this. We also propose approaches to improve LL when ephemeral random constants are used. Furthermore, we adapt a scheme of interleaving runs to alleviate the burden of tuning the population size, a crucial parameter for LL, to SR. We run experiments on 10 real-world datasets, enforcing a strict limitation on solution size, to enable interpretability. We find that the new LL method outperforms the standard one, and that GOMEA outperforms both traditional and semantic GP. We also find that the small solutions evolved by GOMEA are competitive with tuned decision trees, making GOMEA a promising new approach to SR.

Unconventional scaling of the superfluid density with the critical temperature in transition metal dichalcogenides.

We report on muon spin rotation experiments probing the magnetic penetration depth λ(T) in the layered superconductors in 2H-NbSe2 and 4H-NbSe2. The current results, along with our earlier findings on 1T'-MoTe2 (Guguchia et al.), demonstrate that the superfluid density scales linearly with T c in the three transition metal dichalcogenide superconductors. Upon increasing pressure, we observe a substantial increase of the superfluid density in 2H-NbSe2, which we find to correlate with T c. The correlation deviates from the abovementioned linear trend. A similar deviation from the Uemura line was also observed in previous pressure studies of optimally doped cuprates. This correlation between the superfluid density and T c is considered a hallmark feature of unconventional superconductivity. Here, we show that this correlation is an intrinsic property of the superconductivity in transition metal dichalcogenides, whereas the ratio T c/T F is approximately a factor of 20 lower than the ratio observed in hole-doped cuprates. We, furthermore, find that the values of the superconducting gaps are insensitive to the suppression of the charge density wave state.

Reactivity of tetrahydrobiopterin bound to nitric-oxide synthase.

Levels of tetrahydrobiopterin (BH(4)) bound to nitric-oxide synthase (NOS) were examined during multiple turnovers of the enzyme in the presence of an NADPH-regenerating system. Our findings show that NOS-bound BH(4) does not remain in a static state but undergoes redox reactions. Under these experimental conditions, the redox state of BH(4) was determined by the balance between calcium/calmodulin (Ca(2+)/CaM)-dependent oxidation of BH(4) mediated by the uncoupled formation of superoxide/hydrogen peroxide on the one hand and by reductive regeneration of BH(4) on the other hand. BH(4) oxidation was appreciably increased in the presence of arginine. Levels of NOS-bound BH(4) were also examined under single turnover conditions in the absence of an NADPH-regenerating system and in the presence of added superoxide dismutase and catalase to suppress the accumulation of superoxide and hydrogen peroxide. BH(4) oxidation was again dependent on Ca(2+)/CaM. The insensitivity to superoxide dismutase and catalase suggested that the single turnover oxidation of BH(4) did not proceed through superoxide/peroxide, although the involvement of these oxidants could not be definitively excluded. The amount of BH(4) oxidized was highest in the presence of arginine, and this oxidation significantly exceeded that in the presence of N(G)-hydroxy-L-arginine. The findings that single turnover oxidation of BH(4) is stimulated by arginine in the presence of Ca(2+)/CaM and that BH(4) is regenerated are consistent with a role for the pterin as an electron donor in product formation; this role remains to be defined.

Reactivity of the flavin semiquinone of nitric oxide synthase in the oxygenation of arginine to NG-hydroxyarginine, the first step of nitric oxide synthesis.

Nitric oxide synthase (NOS) is a heme protein that catalyzes the oxygenation of L-arginine in the presence of NADPH to form nitric oxide, L-citrulline and NADP+, and proceeds via two partial reactions: 1) L-Arginine --> NG-hydroxy-L-arginine 2) NG-Hydroxy-L-arginine --> L-citrulline + nitric oxide Calmodulin, FAD, FMN and tetrahydrobiopterin are required for both reactions. Reactions 1 and 2 require the input of 2 and 1 electron equivalents, respectively. Under normal multiple turnover conditions, these electrons are ultimately derived from NADPH. We previously reported that NOS contains an endogenous reductant that, in the absence of NADPH, can support the single-turnover oxygenation of L-arginine to NG-hydroxy-L-arginine and a relatively small amount of L-citrulline [Campos, K. L., Giovanelli, J., and Kaufman, S. (1995) J. Biol. Chem. 270, 1721-1728]. This reductant has now been identified as the stable flavin semiquinone free radical (FSQ). Its oxidation appears to be coupled to the formation of NG-hydroxy-L-arginine and L-citrulline. The rate of FSQ oxidation is two orders of magnitude slower than the flux of electrons from NADPH through NOS during normal turnover of the enzyme, indicating that FSQ is not the proximal electron donor for heme under these conditions.

Reduction of quinonoid dihydrobiopterin to tetrahydrobiopterin by nitric oxide synthase.

Rat cerebellar nitric oxide synthase (NOS) purified from transfected human kidney cells catalyzes an NADPHdependent reduction of quinonoid dihydrobiopterin (qBH2) to tetrahydrobiopterin (BH4). Reduction of qBH2 at 25 microM proceeds at a rate that is comparable with that of the overall reaction (citrulline synthesis) and requires calcium ions and calmodulin for optimal activity; NADH has only 10% of the activity of NADPH. The reduction rate with the quinonoid form of 6-methyldihydropterin is approximately twice that with qBH2. 7,8-Dihydrobiopterin had negligible activity. Neither 7,8-dihydrobiopterin nor BH4 affected the rate of qBH2 reduction. Reduction is inhibited by the flavoprotein inhibitor diphenyleneiodonium, whereas inhibitors of electron transfer through heme (7-nitroindazole and N-nitroarginine) stimulated the rate to a small extent. Methotrexate, which inhibits a variety of enzymes catalyzing dihydrobiopterin reduction, did not inhibit. These studies provide the first demonstration of the reduction of qBH2 to BH4 by NOS and indicate that the reduction is catalyzed by the flavoprotein "diaphorase" activity of NOS. This activity is located on the reductase (C-terminal) domain, whereas the high affinity BH4 site involved in NOS activation is located on the oxygenase (N-terminal) domain. The possible significance of this reduction of qBH2 to the essential role of BH4 in NOS is discussed.

Polyol pools in Aspergillus niger.

The accumulation and excretion of polyols was investigated under various growth conditions and at different stages of the life cycle of Aspergillus niger. Glycerol was found to be the major solute in osmotic adjustment of the hyphae. Conidiospores contain large amounts of mannitol, which are rapidly metabolized during early germination, leading to the accumulation of glycerol. Glycerol is the major polyol in young mycelium, whereas in older mycelium mannitol and erythritol predominate. In all experiments, polyols were also excreted. The mechanism and function of this process is unknown, but it might be a way to control the levels of the intracellular polyol pools. Polyols are rapidly taken up again upon starvation. In a glycerol kinase mutant the synthesis of glycerol is unaffected but the excreted level of the polyol is higher. This glycerol is taken up again upon starvation, and accumulates intracellularly as it can not be metabolized further.

Characterization of an Aspergillus nidulans L-arabitol dehydrogenase mutant.

The degradation pathway for L-arabinose, which consists of a sequence of alternating reduction and oxidation reactions prior to ultimate phosphorylation, was studied in Aspergillus nidulans wild-type as well as in an L-arabinose non-utilizing mutant. The inability of the mutant to use L-arabinose was caused by the absence of L-arabitol dehydrogenase activity. The effect of the mutation on polyol accumulation patterns was studied upon growth on various carbon sources. The presence of L-arabinose resulted in intracellular accumulation of arabitol in this mutant. Moreover, the mutant secreted arabitol under these conditions and, in contrast to the wild-type, featured enhanced expression of enzymes involved in L-arabinose catabolism as well as of extracellular glycosyl hydrolases involved in degradation of the plant cell wall polysaccharide L-arabinan.

Localization of Glucose Oxidase and Catalase Activities in Aspergillus niger.

The subcellular localization of glucose oxidase (EC 1.1.3.4) in Aspergillus niger N400 (CBS 120.49) was investigated by (immuno)cytochemical methods. By these methods, the bulk of the enzyme was found to be localized in the cell wall. In addition, four different catalases (EC 1.11.1.6) were demonstrated by nondenaturing polyacrylamide gel electrophoresis of crude extracts of induced and noninduced cells. Comparison of both protoplast and mycelial extracts indicated that, of two constitutive catalases, one is located outside the cell membrane whereas the other is intracellular. Parallel with the induction of glucose oxidase, two other catalases are also induced, one located intracellularly and one located extracellularly. Furthermore, lactonase (EC 3.1.1.17) activity, catalyzing the hydrolysis of glucono-delta-lactone to gluconic acid, was found to be exclusively located outside the cell membrane, indicating that gluconate formation in A. niger occurs extracellularly.

Glycerol catabolism in Aspergillus nidulans.

Glycerol is catabolized in Aspergillus nidulans by glycerol kinase and a mitochondrial FAD-dependent sn-glycerol 3-phosphate dehydrogenase. The levels of both enzymes are controlled by carbon catabolite repression and by specific induction. Biochemical and genetical analyses show that dihydroxyacetone and D-glyceraldehyde are converted into glycerol and then catabolized by the same pathway. D-Glyceraldehyde can be reduced by NADP(+)-dependent glycerol dehydrogenase or by alcohol dehydrogenase I, while dihydroxyacetone is only reduced by the first enzyme. Three new glycerol non-utilizing mutants have been found. These three mutations define three hitherto unknown loci, glcE, glcF and glcG. The mutation in glcG leads to a greatly decreased sn-glycerol-3-phosphate dehydrogenase activity.

Genetic localization of a series of genes affecting glucose oxidase levels in Aspergillus niger.

A number of mutants of Aspergillus niger, affected in glucose oxidase (GOX) expression, are described. The overproducing mutants could be classified into seven complementation groups whereas two glucose oxidase-negative complementation groups were recognized. These nine gox loci were assigned to linkage groups using master strains with marked chromosomes. Three gox loci are in linkage group II, one is in III, two are in V and two are in linkage group VII. One weak glucose oxidase-overproducing mutant could not be assigned to one of the linkage groups. These genetically well characterized mutants will be used in a strain improvement program based on genetic recombination.

Characterization of a glycerol kinase mutant of Aspergillus niger.

A glycerol-kinase-deficient mutant of Aspergillus niger was isolated. Genetic analysis revealed that the mutation is located on linkage group VI. The phenotype of this mutant differed from that of a glycerol kinase mutant of Aspergillus nidulans in its ability to utilize dihydroxyacetone (DHA). The weak growth on glycerol of the A. niger glycerol kinase mutant showed that glycerol phosphorylation is an important step in glycerol catabolism. The mutant could still grow normally on DHA because of the presence of a DHA kinase. This enzyme, probably in combination with an NAD(+)-dependent glycerol dehydrogenase, present only in the mutant, is responsible for the weak growth of the mutant on glycerol. Enzymic analysis of both the mutant and the parental strain showed that at least three different glycerol dehydrogenases were formed under different physiological conditions: the NAD(+)-dependent enzyme described above, a constitutive NADP(+)-dependent enzyme and a D-glyceraldehyde-specific enzyme induced on D-galacturonate. The glycerol kinase mutant showed impaired growth on D-galacturonate.

Purification and properties of NADP(+)-dependent glycerol dehydrogenases from Aspergillus nidulans and A. niger.

Glycerol dehydrogenase, NADP(+)-specific (EC 1.1.1.72), was purified from mycelium of Aspergillus nidulans and Aspergillus niger using different purification procedures. Both enzymes had an Mr of approximately 38,000 and were immunologically cross-reactive, but had different amino acid compositions and isoelectric points. For both enzymes, the substrate specificity was limited to glycerol and erythritol for the oxidative reaction and to dihydroxyacetone (DHA), diacetyl, methylglyoxal, erythrose and D-glyceraldehyde for the reductive reaction. The A. nidulans enzyme had a turnover number twice that of the A. niger enzyme at pH 6.0, whereas inhibition by NADP+ was less (Ki = 45 microM vs 13 microM). It is proposed that both enzymes catalyse in vivo the reduction of DHA to glycerol and that they are regulated by the anabolic reduction charge.

Structure of the Pseudomonas putida alkBAC operon. Identification of transcription and translation products.

The structural genes of the Pseudomonas oleovorans alk (alkane utilization) system, which are localized on the alkBAC operon, were cloned as a 16.9-kilobase pair EcoRI fragment. We have measured the length and determined the position of the alkBAC operon on this fragment by electron microscopy of R-loops. Furthermore, the 7.3-kilobase pair long alkBAC operon was analyzed for translation products in Escherichia coli minicells. Using a spectrum of overlapping subclones, six different proteins were identified. Starting from the alkBAC promotor, these polypeptides had molecular masses of 41, 15, 49, 58, 59, and 20 kDa, respectively. The 41-kDa protein was identified as alkane hydroxylase by reaction with a specific antibody. The 15- and 49-kDa peptides are soluble components of the alkane hydroxylase complex. The 58-kDa protein is most likely involved in alkanol dehydrogenase activity.