A magnetic lens for cold atoms controlled by a rf field

We report on a new type of magnetic lens that focuses atomic clouds using a static inhomogeneous magnetic field in combination with a radio-frequency field. The experimental study is performed with a cloud of cold cesium atoms. The rf field adiabatically deforms the magnetic potential of a coil and therefore changes its focusing properties. The focal length can be tuned precisely by changing the rf frequency value. Depending on the rf antenna position relative to the DC magnetic profile, the focal length of the atomic lens can be either decreased or increased by the rf field

Dipolar atomic spin ensembles in a double-well potential

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

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

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

All-Optical Production of Chromium Bose-Einstein Condensates

We report on the production of ^52Cr Bose Einstein Condensates (BEC) with an all-optical method. We first load 5.10^6 metastable chromium atoms in a 1D far-off-resonance optical trap (FORT) from a Magneto Optical Trap (MOT), by combining the use of Radio Frequency (RF) frequency sweeps and depumping towards the ^5S_2 state. The atoms are then pumped to the absolute ground state, and transferred into a crossed FORT in which they are evaporated. The fast loading of the 1D FORT (35 ms 1/e time), and the use of relatively fast evaporative ramps allow us to obtain in 20 s about 15000 atoms in an almost pure condensate.Comment: 4 pages, 4 figure

Rcf2 revealed in cryoEM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes

The organisation of the mitochondrial electron transport chain proteins into supercomplexes (SCs) is now undisputed, however their assembly process, or the role of differential expression isoforms, have yet to be determined. In Saccharomyces cerevisiae, cytochrome c oxidase (CIV) forms SCs of varying stoichiometry with cytochrome bc1 (CIII). Recent studies have revealed, in normoxic condition of growth, an interface made exclusively by Cox5A, the only yeast respiratory protein that exists as one of two isoforms depending on oxygen levels. Here, we present the cryo-EM structures of the III2-IV1 and III2-IV2 SCs containing the hypoxic isoform Cox5B solved at 3.4 and 2.8 Å, respectively. We show that the change of isoform doesn’t affect SC formation or activity and that SC stoichiometry is dictated by the level of CIII/CIV biosynthesis. Comparison of the CIV5B and CIV5A-containing SC structures highlighted few differences, mainly found in the region of Cox5. Additional density was revealed in all SCs, independent of CIV isoform, in a pocket formed by Cox1, Cox3, Cox12 and Cox13, away from the CIII-CIV interface. In the CIV5B-containing hypoxic SCs, this could be confidently assigned to the hypoxia-induced gene 1 (Hig1) type 2 protein Rcf2. With conserved residues in mammalian Hig1 proteins and Cox3/Cox12/Cox13 orthologues, we propose that Hig1 type 2 proteins are stoichiometric subunits of CIV, at least when within a III-IV SC

Thermodynamics of a Bose Einstein condensate with free magnetization

We study thermodynamic properties of a gas of spin 3 52Cr atoms across Bose Einstein condensation. Magnetization is free, due to dipole-dipole interactions (DDIs). We show that the critical temperature for condensation is lowered at extremely low magnetic fields, when the spin degree of freedom is thermally activated. The depolarized gas condenses in only one spin component, unless the magnetic field is set below a critical value, below which a non ferromagnetic phase is favored. Finally we present a spin thermometry efficient even below the degeneracy temperature.Comment: 4 pages, 4 figure

Accumulation and thermalization of cold atoms in a finite-depth magnetic trap

We experimentally and theoretically study the continuous accumulation of cold atoms from a magneto-optical trap (MOT) into a finite depth trap, consisting in a magnetic quadrupole trap dressed by a radiofrequency (RF) field. Chromium atoms (52 isotope) in a MOT are continuously optically pumped by the MOT lasers to metastable dark states. In presence of a RF field, the temperature of the metastable atoms that remain magnetically trapped can be as low as 25 microK, with a density of 10^17 atoms.m-3, resulting in an increase of the phase-space density, still limited to 7.10^-6 by inelastic collisions. To investigate the thermalization issues in the truncated trap, we measure the free evaporation rate in the RF-truncated magnetic trap, and deduce the average elastic cross section for atoms in the 5D4 metastable states, equal to 7.0 10^-16m2.Comment: 9 pages, 10 Figure

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

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

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