1,842 research outputs found

    Antifouling bastadin congeners target blue mussel phenoloxidase and complex copper(II) ions

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    Synthetically prepared congeners of spongederived bastadin derivatives such as 5,5'-dibromohemibastadin- 1 (DBHB) that suppress the settling of barnacle larvae were identified in this study as strong inhibitors of blue mussel phenoloxidase that is involved in the firm attachment of mussels to a given substrate. The IC50 value of DBHB as the most active enzyme inhibitor encountered in this study amounts to 0.84 mu M. Inhibition of phenoloxidase by DBHB is likely due to complexation of copper(II) ions from the catalytic centre of the enzyme by the a-oxo-oxime moiety of the compound as shown here for the first time by structure activity studies and by X-ray structure determination of a copper(II) complex of DBHB.Biotechnology & Applied MicrobiologyMarine & Freshwater BiologySCI(E)EI0ARTICLE61148-11581

    Resonant demagnetization of a dipolar BEC in a 3D optical lattice

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    We study dipolar relaxation of a chromium BEC loaded into a 3D optical lattice. We observe dipolar relaxation resonances when the magnetic energy released during the inelastic collision matches an excitation towards higher energy bands. A spectroscopy of these resonances for two orientations of the magnetic field provides a 3D band spectroscopy of the lattice. The narrowest resonance is registered for the lowest excitation energy. Its line-shape is sensitive to the on-site interaction energy. We use such sensitivity to probe number squeezing in a Mott insulator, and we reveal the production of three-body states with entangled spin and orbital degrees of freedom.Comment: 5 pages, 3 Figures, Supplemental Materia

    Dipolar atomic spin ensembles in a double-well potential

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    We experimentally study the spin dynamics of mesoscopic ensembles of ultracold magnetic spin-3 atoms located in two separated wells of an optical dipole trap. We use a radio-frequency sweep to selectively flip the spin of the atoms in one of the wells, which produces two separated spin domains of opposite polarization. We observe that these engineered spin domains are metastable with respect to the long-range magnetic dipolar interactions between the two ensembles. The absence of inter-cloud dipolar spin-exchange processes reveals a classical behavior, in contrast to previous results with atoms loaded in an optical lattice. When we merge the two subsystems, we observe spin-exchange dynamics due to contact interactions which enable the first determination of the s-wave scattering length of 52Cr atoms in the S=0 molecular channel a_0=13.5^{+11}_{-10.5}a_B (where a_B is the Bohr radius).Comment: 9 pages, 7 figure

    Toward a Common Framework and Database of Materials for Soft Robotics

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    To advance the field of soft robotics, a unified database of material constitutive models and experimental characterizations is of paramount importance. This will facilitate the use of finite element analysis to simulate their behavior and optimize the design of soft-bodied robots. Samples from seventeen elastomers, namely Body Double™ SILK, Dragon Skin™ 10 MEDIUM, Dragon Skin 20, Dragon Skin 30, Dragon Skin FX-Pro, Dragon Skin FX-Pro + Slacker, Ecoflex™ 00–10, Ecoflex 00–30, Ecoflex 00–50, Rebound™ 25, Mold Star™ 16 FAST, Mold Star 20T, SORTA-Clear™ 40, RTV615, PlatSil® Gel-10, Psycho Paint®, and SOLOPLAST 150318, were subjected to uniaxial tensile tests according to the ASTM D412 standard. Sample preparation and tensile test parameters are described in detail. The tensile test data are used to derive parameters for hyperelastic material models using nonlinear least-squares methods, which are provided to the reader. This article presents the mechanical characterization and the resulting material properties for a wide set of commercially available hyperelastic materials, many of which are recognized and commonly applied in the field of soft robotics, together with some that have never been characterized. The experimental raw data and the algorithms used to determine material parameters are shared on the Soft Robotics Materials Database GitHub repository to enable accessibility, as well as future contributions from the soft robotics community. The presented database is aimed at aiding soft roboticists in designing and modeling soft robots while providing a starting point for future material characterizations related to soft robotics research

    Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase

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    In cytochrome c oxidase (CytcO) reduction of O2 to water is linked to uptake of eight protons from the negative side of the membrane: four are substrate protons used to form water and four are pumped across the membrane. In bacterial oxidases, the substrate protons are taken up through the K and the D proton pathways, while the pumped protons are transferred through the D pathway. On the basis of studies with CytcO isolated from bovine heart mitochondria, it was suggested that in mitochondrial CytcOs the pumped protons are transferred though a third proton pathway, the H pathway, rather than through the D pathway. Here, we studied these reactions in S. cerevisiae CytcO, which serves as a model of the mammalian counterpart. We analyzed the effect of mutations in the D (Asn99Asp and Ile67Asn) and H pathways (Ser382Ala and Ser458Ala) and investigated the kinetics of electron and proton transfer during the reaction of the reduced CytcO with O2. No effects were observed with the H pathway variants while in the D pathway variants the functional effects were similar to those observed with the R. sphaeroides CytcO. The data indicate that the S. cerevisiae CytcO uses the D pathway for proton uptake and presumably also for proton pumping

    A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria

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    Mitochondria metabolise almost all of the oxygen that we consume, reducing it to water by cytochrome c oxidase (CcO). CcO maximises energy capture into the protonmotive force by pumping protons across the mitochondrial inner membrane. Forty years after the H+/e- stoichiometry was established, a consensus has yet to be reached on the route taken by pumped protons to traverse CcO’s hydrophobic core and on whether bacterial and mitochondrial CcOs operate via the same coupling mechanism. To resolve this, we exploited the unique amenability to mitochondrial DNA mutagenesis of the yeast S. cerevisiae to introduce single point mutations in the hydrophilic pathways of CcO to test function. From ADP/O ratio measurements on preparations of intact mitochondria, we definitely established that the D-channel, and not the H-channel, is the proton pump of the yeast mitochondrial enzyme, supporting an identical coupling mechanism in all forms of the enzyme
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