Theoretical model investigating the magnetic properties of cobalt-doped ZnO.

We propose a theoretical model to investigate the magnetic properties of cobalt-doped ZnO (ZnO:Co) thin films qualitatively. The model was built on the dilute Co dopants in the host of ZnO forming the magnetic Co+2 ions and the energy level of the magnetic ions crossing the band edge of ZnO resulting in a magnetic interaction between the Co+2 spins and the spins of the electrons from the conduction band of ZnO. The mechanism of the ferromagnetism revealed in the studied system is proposed here to be induced not only by the mediated conducting electrons via spin interactions but also by the Coulomb excitations, arising from the electrons localized by the oxygen vacancies. This approach of including Coulomb excitation in the modified carrier-mediated model could explain well the magnetic properties of ZnO:Co and solves the drawback of the carrier-mediated model in interpreting the appearance of ferromagnetism in the insulating ZnO:Co. We propose that the Coulomb excitations induced by the electrons captured by the oxygen vacancies are an essential element in the magnetic ZnO, which reveals the fact that the bound magnetic polaron model without considering the Coulomb excitation is insufficient to describe the magnetic properties of ZnO.

Growth and optical investigations of high quality individual CdTe/(Cd,Mg)Te core/shell nanowires.

CdTe nanowires with the average diameter of only 40 nm coated with (Cd,Mg)Te shells are grown using Au-catalyzed vapor-liquid-solid growth mechanism in a system for molecular beam epitaxy. High optical quality of individual nanowires is revealed by means of low temperature cathodoluminescence and micro-luminescence. It is found that, the optical emission spectrum consists mostly of the near band edge emission without any significant contribution of defect related luminescence. Moreover, the importance of surface passivation with (Cd,Mg)Te coating shells is demonstrated.

Comparison of magneto-optical properties of various excitonic complexes in CdTe and CdSe self-assembled quantum dots.

We present a comparative study of two self-assembled quantum dot (QD) systems based on II-VI compounds: CdTe/ZnTe and CdSe/ZnSe. Using magneto-optical techniques we investigated a large population of individual QDs. The systematic photoluminescence studies of emission lines related to the recombination of neutral exciton X, biexciton XX, and singly charged excitons (X(+), X(-)) allowed us to determine average parameters describing CdTe QDs (CdSe QDs): X-XX transition energy difference 12 meV (24 meV); fine-structure splitting δ1=0.14 meV (δ1=0.47 meV); g-factor g = 2.12 (g = 1.71); diamagnetic shift γ=2.5 µeV T(-2) (γ =1.3 µeV T(-2)). We find also statistically significant correlations between various parameters describing internal structure of excitonic complexes.

Coexistence of optically active radial and axial CdTe insertions in single ZnTe nanowire.

We report on the growth, cathodoluminescence and micro-photoluminescence of individual radial and axial CdTe insertions in ZnTe nanowires. In particular, the cathodoluminescence technique is used to determine the position of each emitting object inside the nanowire. It is demonstrated that depending on the CdTe deposition temperature, one can obtain an emission either from axial CdTe insertions only, or from both, radial and axial heterostructures, simultaneously. At 350 °C CdTe grows only axially, whereas at 310 °C and 290 °C, there is also significant deposition on the nanowire sidewalls resulting in radial core/shell heterostructures. The presence of Cd atoms on the sidewalls is confirmed by energy dispersive X-ray spectroscopy. Micro-photoluminescence study reveals a strong linear polarization of the emission from both types of heterostructures in the direction along the nanowire axis.

Coherent Precession of an Individual 5/2 Spin.

We present direct observation of a coherent spin precession of an individual Mn^{2+} ion, having both electronic and nuclear spins equal to 5/2, embedded in a CdTe quantum dot and placed in a magnetic field. The spin state evolution is probed in a time-resolved pump-probe measurement of absorption of the single dot. The experiment reveals subtle details of the large-spin coherent dynamics, such as nonsinusoidal evolution of states occupation, and beatings caused by the strain-induced differences in energy levels separation. Sensitivity of the large-spin impurity on the crystal strain opens the possibility of using it as a local strain probe.

Activation of an intense near band edge emission from ZnTe/ZnMgTe core/shell nanowires grown on silicon.

The absence of luminescence in the near band edge energy region of Te-anion based semiconductor nanowires grown by gold catalyst assisted molecular beam epitaxy has strongly limited their applications in the field of photonics. In this paper, an enhancement of the near band edge emission intensity from ZnTe/ZnMgTe core/shell nanowires grown on Si substrates is reported. A special role of the use of Si substrates instead of GaAs substrates is emphasized, which results in an increase of the near band edge emission intensity by at least one order of magnitude accompanied by a simultaneous reduction of the defect related luminescence. A possible explanation of this effect relies on the presence of Ga-related deep level defects in structures grown on GaAs substrates, which are absent when Si substrates are used. Monochromatic mapping of the cathodoluminescence clearly confirms that the observed emission originates, indeed, from the ZnTe/ZnMgTe core/shell nanowires, whereas individual objects are studied by means of microphotoluminescence.

Quantum interference in exciton-Mn spin interactions in a CdTe semiconductor quantum dot.

We show theoretically and experimentally the existence of a new quantum-interference effect between the electron-hole interactions and the scattering by a single Mn impurity. The theoretical model, including electron-valence-hole correlations, the short- and long-range exchange interaction of a Mn ion with the heavy hole and with electron and anisotropy of the quantum dot, is compared with photoluminescence spectroscopy of CdTe dots with single magnetic ions. We show how the design of the electronic levels of a quantum dot enables the design of an exciton, control of the quantum interference, and hence engineering of light-Mn interaction.

Optical manipulation of a single Mn spin in a CdTe-based quantum dot.

Two coupled CdTe quantum dots, selected from a self-assembled system, one of them containing a single Mn ion, were studied by continuous wave and modulated photoluminescence, photoluminescence excitation, and photon correlation experiments. Optical writing of information on the spin state of the Mn ion has been demonstrated, using the orientation of the Mn spin by spin-polarized carriers transferred from the neighboring quantum dot. Mn spin orientation time values from 20 to 100 ns were measured, depending on the excitation power. Storage time of the information on the Mn spin was found to be enhanced by application of a static magnetic field of 1 T, reaching hundreds of microseconds in the dark. Simple rate equation models were found to describe correctly the static and dynamical properties of the system.

Size-dependent magneto-optical effects in CdMnTe diluted magnetic quantum dots.

We report on the growth and high spatial resolution magneto-photoluminescence of CdMnTe quantum dots embedded in a ZnCdTe matrix with Mn content of about 3%. The giant Zeeman spitting of excitonic emission coming from individual quantum dots and magnetization fluctuations inside them are studied in magnetic fields up to 7 T. We have found that the description of these effects requires the inclusion of antiferromagnetic Mn-Mn interaction in the considerations. Moreover, the values of the Zeeman shift are strongly related to the size of the dot. In particular, the higher spectral position of the line is, i.e., the smaller the dot, the smaller the Zeeman splitting that is observed. This effect is quantitatively explained with model calculations made under the assumption of magnetic polaron formation in diluted magnetic quantum dots and the presence of ion-ion exchange interaction.

The N-terminal part of recombinant human tear lipocalin/von Ebner's gland protein confers cysteine proteinase inhibition depending on the presence of the entire cystatin-like sequence motifs.

Human Tear Lipocalin/von Ebner's gland protein (TL) is a member of the lipocalin superfamily. The protein is secreted by a number of serous glands and tissues and is overproduced under conditions of stress, infection and inflammation. In addition to its typical affinity for lipophilic ligands it was recently found to be able to inhibit cysteine proteinases [van't Hof et al., J. Biol. Chem. 272 (1997), 1837-1841], probably due to the presence of amino acid motifs resembling the papain binding domains of family 2 cystatins. In this work we have used a recombinant protein to confirm the results obtained with native TL. The inhibitory activity of the recombinant protein against papain was dependent on the ratio of papain and TL. At higher papain concentrations, the N-terminal sequence of TL was cleaved off by the protease, indicating that it can act in an inhibitor- or a substrate-like mode. This behaviour resembles that observed with certain chicken cystatin mutants. Using a recombinant TL mutant we found that the two Leu residues (Leu4-Leu5) contained within the first cystatin-like motif are absolutely essential for the inhibitory activity. These results were supported by experiments using a recombinant form of the corresponding pig von Ebner's gland protein (VEGp). This protein, which does not possess a fully conserved first cystatin-like motif, is unable to inhibit papain.

Human tear lipocalin acts as an oxidative-stress-induced scavenger of potentially harmful lipid peroxidation products in a cell culture system.

Human tear lipocalin [lipocalin 1 (lcn-1); von Ebner's gland protein] is a member of the lipocalin superfamily that is known to bind an unusual variety of lipophilic ligands. Because of its properties and its tissue-specific expression it has been suggested that lcn-1 might act as a physiological protection factor of epithelia. Overexpression of lcn-1 under certain disease conditions supported such a function. However, experimental investigations into its exact biological role and its mode of expression were impeded because lcn-1 was previously found to be produced only in serous glands. To overcome this problem we therefore sought a cell line that produced lcn-1 endogenously. Using reverse-transcriptase-mediated PCR analysis we found expression of lcn-1 in the human teratocarcinoma-derived NT2 precursor cells. Under normal conditions the production of lcn-1 is low. However, treatment of the cells with H(2)O(2) or FeSO(4), which typically induce lipid peroxidation, significantly enhanced the expression of lcn-1. Binding studies revealed that arachidonic acid and several lipid peroxidation products including 7beta-hydroxycholesterol, 8-isoprostane and 13-hydroxy-9,11-octadecadienoic acid specifically bind to lcn-1. To investigate the physiological consequence of this observation we purified holo-(lcn-1) from culture medium and extracted the bound ligands. The presence of F(2)-isoprostanes in the extracts obtained from the fractions containing lcn-1 indicates that these typical lipid peroxidation products are indeed ligands of the protein in vivo. These results support the idea that lcn-1 acts as a physiological scavenger of potentially harmful lipophilic molecules; lcn-1 might therefore be a novel member of the cellular defence against the deleterious effects of oxidative stress.

Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display.

Human lipocalin-1 (Lcn-1, also called tear lipocalin), a member of the lipocalin structural superfamily, is produced by a number of glands and tissues and is known to bind an unusually large array of hydrophobic ligands. Apart from its specific function in stabilizing the lipid film of human tear fluid, it is suggested to act as a physiological scavenger of potentially harmful lipophilic compounds, in general. To characterize proteins involved in the reception, detoxification, or degradation of these ligands, a cDNA phage-display library from human pituitary gland was constructed and screened for proteins interacting with Lcn-1. Using this method an Lcn-1 interacting phage was isolated that expressed a novel human protein. Molecular cloning and analysis of the entire cDNA indicated that it encodes a 55-kDa protein, lipocalin-1 interacting membrane receptor (LIMR), with nine putative transmembrane domains. The cell membrane location of this protein was confirmed by immunocytochemistry and Western blot analysis of membrane fractions of human NT2 cells. Independent biochemical investigations using a recombinant N-terminal fragment of LIMR also demonstrated a specific interaction with Lcn-1 in vitro. Based on these data, we suggest LIMR to be a receptor of Lcn-1 ligands. These findings constitute the first report of cloning of a lipocalin interacting, plasma membrane-located receptor, in general. In addition, a sequence comparison supports the biological relevance of this novel membrane protein, because genes with significant nucleotide sequence similarity are present in Takifugu rubripes, Drosophila melanogaster, Caenorhabditis elegans, Mus musculus, Bos taurus, and Sus scrofa. According to data derived from the human genome sequencing project, the LIMR-encoding gene has to be mapped on human chromosome 12, and its intron/exon organization could be established. The entire LIMR-encoding gene consists of about 13.7 kilobases in length and contains 16 introns with a length between 91 and 3438 base pairs.

Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding.

Human tear lipocalin (TL) is an unusual member of the lipocalin protein family, since it is known to bind a large variety of lipophilic ligands in vivo and acts as a cysteine proteinase inhibitor in vitro. It is suggested to function as a physiological protection factor by scavenging lipophilic potentially harmful compounds. Since protein-protein interaction or macromolecular complexation is a common feature of many lipocalins, we applied phage display technology to identify TL interacting proteins. By panning of a human prostate cDNA phagemid library against purified TL we isolated a thioredoxin (Trx) encoding phage clone. Biochemical analysis revealed that TL indeed interacts with Trx and is reduced by this redox protein. Reduction of the TL-specific disulfide bond is of functional relevance, since the reduced protein shows a nine-fold increase in ligand affinity when tested with retinoic acid as ligand.

Complement component C8gamma is expressed in human fetal and adult kidney independent of C8alpha.

Human complement component C8gamma is an unusual complement factor since it shows no homology to other complement proteins but is a member of the lipocalin superfamily. So far, it has been found exclusively in plasma, covalently linked to C8alpha by disulfide bridging. We have used dot blot and Northern blot analyses of a large number of different human tissues to survey systematically the expression pattern of C8gamma. Our experiments clearly showed that besides in liver, this gene is also expressed in fetal and adult kidney. Renal expression of C8gamma is not dependent on C8alpha expression, since we could not detect C8alpha expression in kidney. Thus its physiological function is not restricted to a specific action in association with complement components. As a prerequisite for further characterization of the structure and binding activities of the uncomplexed C8gamma, we have expressed the encoding cDNA in Escherichia coli. To increase the probability for proper folding of the characteristic intramolecular disulfide bridge the recombinant protein was produced by secretion to the periplasm.

Identification of a lipocalin in mucosal glands of the human tracheobronchial tree and its enhanced secretion in cystic fibrosis.

Members of the lipocalin protein family are characterized by their ability to bind small hydrophobic molecules. Some of them are known to be produced by various glands and secretory cells. Under certain conditions, these proteins would be ideally suited for clearance of lipophilic, potentially harmful substances and might also act as protection factors in airway secretions. We therefore used RT-PCR analysis with a set of oligonucleotide primers deduced from conserved regions of lipocalin members to identify specific RNA isolated from human trachea. With two of these oligonucleotide primers, a positive result was obtained. Sequencing of the RT-PCR products revealed that the DNA fragments were identical to the lipocalin 1 (LCN1) encoding cDNA. LCN1 is an unusual lipocalin member that binds a variety of lipophilic compounds and exhibits cysteine proteinase inhibitor and antimicrobial activities. The local production and topographic distribution of LCN1 in the human tracheobronchial tree was then investigated by immunoperoxidase staining on thin-layer sections using a specific antiserum. LCN1 was detectable in the acini of serous mucosal glands and sometimes within the glandular lumen, suggesting excretion of the protein. The latter finding was tested and verified by Western blot analysis of bronchial secretions of healthy individuals. Furthermore, the results of SDS-PAGE and Western blot analysis of bronchial secretions from patients with cystic fibrosis (CF), which are usually characterized by an increase of airway lipids, suggested that LCN1 secretion was enhanced. Northern blot analysis of RNA from normal trachea and RNA isolated from tracheal biopsies of patients with CF indicated that induced secretion was due to an up-regulated expression of the LCN1 gene. Thus, our investigations present the first clear evidence that LCN1 is induced in infection or inflammation and support the idea that this lipocalin functions as a physiologic protection factor of epithelia in vivo.

Structure and organization of the porcine LCN1 gene encoding Tear lipocalin/von Ebner's gland protein.

We have cloned and sequenced the entire genomic fragment of the porcine LCN1 gene which encodes Tear lipocalin/von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in porcine lachrymal and lingual glands. The porcine LCN1 gene is approximately 4.6 kb in size and contains six protein-coding exons and a 3'-nontranslated exon. The structure of this porcine gene is highly similar, in terms of numbers of exons/introns, in size of exons and in intron phasing, to that of the human LCN1 and rat VEGP genes, thus supporting a very close evolutionary relationship of these genes. Within the promoter region of the porcine LCN1 a putative TATA box, a CAAT box and two MRE motifs are found. The same MRE motifs are conserved in the human LCN1 promoter, suggesting that they might be of relevance for LCN1 gene expression. However, additional motifs present in the human LCN1 promoter, such as AP-1 and AP-2 sites, a NF-kappaB site, and a cAMP-responsive element, could not be detected in the porcine LCN1 promoter.