Coherent long-distance displacement of individual electron spins.

Controlling nanocircuits at the single electron spin level is a possible route for large-scale quantum information processing. In this context, individual electron spins have been identified as versatile quantum information carriers to interconnect different nodes of a spin-based semiconductor quantum circuit. Despite extensive experimental efforts to control the electron displacement over long distances, maintaining electron spin coherence after transfer remained elusive up to now. Here we demonstrate that individual electron spins can be displaced coherently over a distance of 5 µm. This displacement is realized on a closed path made of three tunnel-coupled lateral quantum dots at a speed approaching 100 ms-1. We find that the spin coherence length is eight times longer than expected from the electron spin coherence without displacement, pointing at a process similar to motional narrowing observed in nuclear magnetic resonance experiments. The demonstrated coherent displacement will open the route towards long-range interaction between distant spin qubits.The spin states of electrons in quantum dots have well-established potential for use as qubits but some proposed developments require the ability to move the quantum spin state across a larger device. Here, the authors experimentally demonstrate coherent shuttling of spins in a ring of three dots.

Fast spin information transfer between distant quantum dots using individual electrons.

Transporting ensembles of electrons over long distances without losing their spin polarization is an important benchmark for spintronic devices. It usually requires injecting and probing spin-polarized electrons in conduction channels using ferromagnetic contacts or optical excitation. In parallel with this development, important efforts have been dedicated to achieving control of nanocircuits at the single-electron level. The detection and coherent manipulation of the spin of a single electron trapped in a quantum dot are now well established. Combined with the recently demonstrated control of the displacement of individual electrons between two distant quantum dots, these achievements allow the possibility of realizing spintronic protocols at the single-electron level. Here, we demonstrate that spin information carried by one or two electrons can be transferred between two quantum dots separated by a distance of 4 µm with a classical fidelity of 65%. We show that at present it is limited by spin flips occurring during the transfer procedure before and after electron displacement. Being able to encode and control information in the spin degree of freedom of a single electron while it is being transferred over distances of a few micrometres on nanosecond timescales will pave the way towards 'quantum spintronics' devices, which could be used to implement large-scale spin-based quantum information processing.

Transmission phase in the Kondo regime revealed in a two-path interferometer.

We report on the direct observation of the transmission phase shift through a Kondo correlated quantum dot by employing a new type of two-path interferometer. We observed a clear π/2-phase shift, which persists up to the Kondo temperature TK. Above this temperature, the phase shifts by more than π/2 at each Coulomb peak, approaching the behavior observed for the standard Coulomb blockade regime. These observations are in remarkable agreement with two-level numerical renormalization group calculations. The unique combination of experimental and theoretical results presented here fully elucidates the phase evolution in the Kondo regime.

Effect of disorder on the quantum coherence in mesoscopic wires.

We present phase coherence time measurements in quasi-one-dimensional mesoscopic wires made from high mobility two-dimensional electron gas. By implanting gallium ions into a GaAs/AlGaAs heterojunction we are able to vary the diffusion coefficient over 2 orders of magnitude. We show that in the diffusive limit, the decoherence time follows a power law as a function of diffusion coefficient as expected by theory. When the disorder is low enough so that the samples are semiballistic, we observe a new and unexpected regime in which the phase coherence time is independent of disorder. In addition, for all samples the temperature dependence of the phase coherence time follows a power law down to the lowest temperatures without any sign of saturation and this strongly suggests that the frequently observed low temperature saturation is not intrinsic.

Kondo decoherence: finding the right spin model for iron impurities in gold and silver.

We exploit the decoherence of electrons due to magnetic impurities, studied via weak localization, to resolve a long-standing question concerning the classic Kondo systems of Fe impurities in the noble metals gold and silver: which Kondo-type model yields a realistic description of the relevant multiple bands, spin, and orbital degrees of freedom? Previous studies suggest a fully screened spin S Kondo model, but the value of S remained ambiguous. We perform density functional theory calculations that suggest S=3/2. We also compare previous and new measurements of both the resistivity and decoherence rate in quasi-one-dimensional wires to numerical renormalization group predictions for S=1/2, 1, and 3/2, finding excellent agreement for S=3/2.

Scaling of the low-temperature dephasing rate in Kondo systems.

We present phase coherence time measurements in quasi-one-dimensional Ag wires doped with Fe Kondo impurities of different concentrations n_{s}. Because of the relatively high Kondo temperature T_{K} approximately 4.3 K of this system, we are able to explore a temperature range from above T_{K} down to below 0.01T_{K}. We show that the magnetic contribution to the dephasing rate gamma_{m} per impurity is described by a single, universal curve when plotted as a function of T/T_{K}. For T>0.1T_{K}, the dephasing rate is remarkably well described by recent numerical results for spin S=1/2 impurities. At lower temperature, we observe deviations from this theory. Based on a comparison with theoretical calculations for S>1/2, we discuss possible explanations for the observed deviations.

Quantum frustration in the "spin liquid" phase of two-dimensional 3He.

We have measured the ultralow temperature and low field magnetic susceptibility of the 4/7 phase of two-dimensional 3He adsorbed on graphite preplated by one layer of 4He. The experiments are performed by progressively adding 4He to the system, thus suppressing in a controlled way the 3He atoms trapped in substrate heterogeneities. This procedure enables us to determine the intrinsic properties of this spin 1/2 model magnet in the zero field limit. The results show quantitatively that the system is strongly frustrated by multiple spin exchange interactions. A characteristic gapped spin liquid behavior is observed at ultralow temperature.

Characterization of a red beet protein homologous to the essential 36-kilodalton subunit of the yeast V-type ATPase.

V-type proton-translocating ATPases (V-ATPases) (EC 3.6.1.3) are electrogenic proton pumps involved in acidification of endomembrane compartments in all eukaryotic cells. V-ATPases from various species consist of 8 to 12 polypeptide subunits arranged into an integral membrane proton pore sector (Vo) and a peripherally associated catalytic sector (V1). Several V-ATPase subunits are functionally and structurally conserved among all species examined. In yeast, a 36-kD peripheral subunit encoded by the yeast (Saccharomyces cerevisiae) VMA6 gene (Vma6p) is required for stable assembly of the Vo sector as well as for V1 attachment. Vma6p has been characterized as a nonintegrally associated Vo subunit. A high degree of sequence similarity among Vma6p homologs from animal and fungal species suggest that this subunit has a conserved role in V-ATPase function. We have characterized a novel Vma6p homolog from red beet (Beta vulgaris) tonoplast membranes. A 44-kD polypeptide cofractionated with V-ATPases upon gel-filtration chromatography of detergent-solubilized tonoplast membranes and was specifically cross-reactive with anti-Vma6p polyclonal antibodies. The 44-kD polypeptide was dissociated from isolated tonoplast preparations by mild chaotropic agents and thus appeared to be nonintegrally associated with the membrane. The putative 44-kD homolog appears to be structurally similar to yeast Vma6p and occupies a similar position within the holoenzyme complex.

Ras-GTP regulation is not altered in cultured melanocytes with reduced levels of neurofibromin derived from patients with neurofibromatosis 1 (NF1).

As derivatives of the neural crest, epidermal melanocytes are supposed to be clinically affected by NF1 gene defects. The NF1 gene shares sequence homology with the p120 GTPase activating protein (p120-GAP) and neurofibromin has been shown to participate in Ras-regulation. By immunoprecipitation and Western blotting, neurofibromin was found to be expressed in melanocytes from the unaffected skin and café au lait macules of NF1 patients, but the intensity of the neurofibromin band was decreased compared to control cultures. The Ras-GTP/Ras-GDP ratios of NF1 derived melanocyte cultures were comparable to those derived from healthy donors. Furthermore, the total GAP-activity of cell lysates was not altered in NF1 melanocyte cultures compared to controls. However, lysates of proliferating melanocytes, both from NF1 patients and from healthy donors, showed an about 2-fold higher GAP-activity than poorly growing cells. Neurofibromin contributed approximately one third of total GAP-activity, in both control and NF1 melanocytes, indicating that it is not the major regulator of Ras in these cells. These results suggest that the function of neurofibromin in melanocytes is not limited to regulation of Ras activity.

Astrocytes in the nonmyelinated lamina cribrosa of the rat are less polarized than in the optic nerve proper: a freeze-fracture study.

Astrocytes in the lamina cribrosa of the adult rat optic nerve which is devoid of myelination were investigated by means of quantitative freeze-fracturing. The orthogonal arrays of particles (OAPs) were found to be less concentrated in the membranes of subpial endfeet when compared to the OAP concentration in endfeet of the optic nerve proper. This result corresponds to that found previously in the myelin deficient rat (Rohlmann et al: Glia 5:259, 1992) suggesting that lack of myelination generally correlates with altered astrocytes.

The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector.

The yeast vacuolar membrane proton-translocating ATPase (V-ATPase) is a multisubunit complex comprised of peripheral catalytic, and integral membrane domains. At least eight proteins cofractionate with purified preparations of the enzyme including 100-, 69-, 60-, 42-, 36-, 32-, 27-, and 17-kDa polypeptides (Kane, P.M., Yamashiro, C.T., and Stevens, T.H. (1989a) J. Biol. Chem. 264, 19236-19244). We took a reverse genetic approach to clone the structural gene for the 36-kDa subunit of the V-ATPase, VMA6, vma6 null mutants displayed growth characteristics typical of other vma mutants including sensitivity to media buffered at neutral pH or media containing 100 mM Ca2+. Vacuolar acidification was defective in vma6 cells and isolated vacuolar membrane preparations contained no detectable V-ATPase activity. The VMA6 gene encodes a hydrophilic polypeptide of 345 amino acids (predicted molecular mass 39.8-kDa). We present evidence that the VMA6 gene product (Vma6p) is a non-integral membrane component of the membrane pore domain and is required for V-ATPase complex assembly. Vma6p was removed from wild type vacuolar membranes by strong chaotropic agents such as alkaline Na2CO3 or 5M urea, which did not remove integral membrane polypeptides. In yeast cells lacking the integral membrane portion of the V-ATPase complex, Vma6p was unable to stably associate with vacuolar membranes. Conversely, in mutants specifically lacking Vma6p, components of the V-ATPase integral membrane domain were destabilized, and peripheral subunits failed to assemble onto vacuolar membranes. These results are discussed in the context of a developing model for V-ATPase assembly in yeast.

Full-length plastocyanin precursor is translocated across isolated thylakoid membranes.

In higher plants, the chloroplastic protein plastocyanin is synthesized as a transit peptide-containing precursor by cytosolic ribosomes and posttranslationally transported to the thylakoid lumen. En route to the lumen, a plastocyanin precursor is first imported into chloroplasts and then further directed across the thylakoid membrane by a second distinct transport event. A partially processed form of plastocyanin is observed in the stroma during import experiments using intact chloroplasts and has been proposed to be the translocation substrate for the second step (Smeekens, S., Bauerle, C., Hageman, J., Keegstra, K., and Weisbeek, P. (1986) Cell 46, 365-375). To further characterize this second step, we have reconstituted thylakoid transport in a system containing in vitro-synthesized precursor proteins and isolated thylakoid membranes. This system was specific for lumenal proteins since stromal proteins lacking the appropriate targeting information did not accumulate in the thylakoid lumen. Plastocyanin precursor was taken up by isolated thylakoids, proteolytically processed to mature size, and converted to holo form. Translocation was temperature-dependent and was stimulated by millimolar levels of ATP but did not strictly require the addition of stromal factors. We have examined the substrate requirements of thylakoid translocation by testing the ability of different processed forms of plastocyanin to transport in the in vitro system. Interestingly, only the full-length plastocyanin precursor, not the partially processed intermediate form, was competent for transport in this in vitro system.

Kinetic analysis of the transport of thylakoid lumenal proteins in experiments using intact chloroplasts.

The transport of the lumenal protein plastocyanin has been proposed to occur in two steps: 1) transport across the chloroplastic envelope to the stroma and 2) transport across the thylakoid membrane to the lumen where proteolytic maturation occurs. A partially processed stromal form of plastocyanin has been tentatively identified as a pathway intermediate and as the substrate for the second translocation step (Smeekens, S., Bauerle, C., Hageman, J., Keegstra, K., and Weisbeek, P. (1986) Cell 46, 365-375). In this study, we have examined the transport kinetics of several lumenal proteins under various incubation conditions. Soluble intermediate sized forms were observed in import reactions with plastocyanin precursors from three higher plant species and with the precursor of the 33-kDa polypeptide of the oxygen-evolving enhancer complex. The accumulation patterns observed for these soluble intermediate sized forms depended on incubation conditions and could not be consistently explained by a simple model where the intermediate sized form is the substrate for the second step. Thus, it has not been possible to clearly identify the substrate for thylakoid translocation in organello.

Metal-ion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts.

Most chloroplastic proteins are cytosolically synthesized and posttranslationally transported to their proper locations. Two examples of this group of proteins are ferredoxin and plastocyanin, both of which are metal-containing components of the photosynthetic electron-transport chain. The import process for these two proteins includes the insertion of the metal ions to produce the holo forms of the proteins. We show here that in vitro translated precursor proteins of ferredoxin and plastocyanin are synthesized as apo forms and are assembled into their respective holo forms after being imported into isolated chloroplasts. We also provide evidence that only mature-sized proteins are competent to be assembled into holo forms.

Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes.

The energy requirements for the import of nuclear-encoded proteins into isolated chloroplasts have been reinvestigated. We have shown that, in contrast to protein import into mitochondria, the translocation of the precursors to ferredoxin, plastocyanin (prPC) and the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (prSS) across all chloroplastic membranes is independent of a protonmotive force and requires only ATP. This extends previous works in which investigations were limited to prSS and demonstrates that our results are probably general to all chloroplastic protein precursors. Our results are particularly interesting for the import of prPC, since in addition to the two envelope membranes, this protein must traverse the energy-transducing thylakoid membranes en route to its proper location in the thylakoid lumen. This lack of involvement of a protonmotive force, specifically of a transmembrane electric potential, demonstrates that separate mechanisms operate during the import of proteins into chloroplasts and mitochondria. We also examined the question of whether ATP is utilized inside or outside of chloroplasts during protein import. Previous attempts to resolve this question have resulted in conflicting answers. We found, by two independent approaches, that ATP for protein import is utilized inside chloroplasts. The implications of these results on the possible mechanisms of protein import into chloroplasts are discussed.

[Differentiation of existential guilt and compassion in relation to responsibility induction: a film experiment]. / Zur Differenzierung von Existentieller Schuld und Mitleid über Verantwortlichkeitsinduktion: ein Filmexperiment.

Feelings of existential guilt are assumed to depend on the perception of a causal relationship between one's own behavior or (privileged) situation and the disadvantages of others. By contrast, pity should not depend on such perceptions. This hypothesis, which has been supported so far only by correlational studies, was tested experimentally. Eighty students were shown a film about a developing country. The film was provided with four different comments, each representing one experimental condition (between-subjects design). Experimental factors were "amount of misery of the people shown" and "subject's responsibility for these peoples' conditions of life". As expected, subjects in the condition "misery and responsibility" reported higher feelings of guilt, though no more pity than subjects in the remaining three treatment conditions (experiment 1, n = 40). This mean difference, however, was statistically significant for men only. Contrary to our theoretical expectations--and to finding from other experiments on vicarious reparation--the induction of guilt had no effect on willingness to help a third party (experiment 2, n = 40). Possible reasons for this unexpected finding are suggested.

Import into chloroplasts of a yeast mitochondrial protein directed by ferredoxin and plastocyanin transit peptides.

Many chloroplast proteins are synthesized in the cytoplasm as precursors which contain an amino terminal transit peptide. These precursors are subsequently imported into chloroplast and targeted to one of several organellar locations. This import is mediated by the transit peptide, which is cleaved off during import. We have used the transit peptides of ferredoxin (chloroplast stroma) and plastocyanin (thylakoid lumen) to study chloroplast protein import and intra-organellar routing toward different compartments. Chimeric genes were constructed that encode precursor proteins in which the transit peptides are linked to yeast mitochondrial manganese superoxide dismutase. Chloroplast protein import and localization experiments show that both chimeric proteins are imported into the chloroplast stroma and processed. The plastocyanin transit sequence did not direct superoxide dismutase to the thylakoids; this protein was found in the stroma as an intermediate that still contains part of the plastocyanin transit peptide. The organelle specificity of these chimeric precursors reflected the transit peptide parts of the molecules, because neither the ferredoxin and plastocyanin precursors nor the chimeric proteins were imported into isolated yeast mitochondria.