Refine
Year of publication
- 2022 (77) (remove)
Language
- English (77)
Has Fulltext
- yes (77)
Is part of the Bibliography
- no (77)
Keywords
Institute
- Physik (73)
- Frankfurt Institute for Advanced Studies (FIAS) (63)
- Informatik (59)
- Biochemie und Chemie (2)
- Biochemie, Chemie und Pharmazie (2)
- MPI für Biophysik (2)
- Medizin (2)
Annihilation dynamics plays a fundamental role in the baryon−antibaryon interaction (B−B¯¯¯¯) at low-energy and its strength and range are crucial in the assessment of possible baryonic bound states. Experimental data on annihilation cross sections are available for the p−p¯¯¯ system but not in the low relative momentum region. Data regarding the B−B¯¯¯¯ interaction with strange degrees of freedom are extremely scarce, hence the modeling of the annihilation contributions is mainly based on nucleon−antinucleon (N−N¯¯¯¯) results, when available. In this letter we present a measurement of the p−p¯¯¯, p−Λ¯¯¯¯⊕p¯¯¯−Λ and Λ−Λ¯¯¯¯ interaction using correlation functions in the relative momentum space in high-multiplicity triggered pp collisions at s√=13 TeV recorded by ALICE at the LHC. In the p−p¯¯¯ system the couplings to the mesonic channels in different partial waves are extracted by adopting a coupled-channel approach with recent χEFT potentials. The inclusion of these inelastic channels provides good agreement with the data, showing a significant presence of the annihilation term down to zero momentum. Predictions obtained using the Lednický−Lyuboshits formula and scattering parameters obtained from heavy-ion collisions, hence mainly sensitive to elastic processes, are compared with the experimental p−Λ¯¯¯¯⊕p¯¯¯−Λ and Λ−Λ¯¯¯¯ correlations. The model describes the Λ−Λ¯¯¯¯ data and underestimates the p−Λ¯¯¯¯⊕p¯¯¯−Λ data in the region of momenta below 200 MeV/c. The observed deviation indicates a different contribution of annihilation channels to the two systems containing strange hadrons.
Measurements of event-by-event fluctuations of charged-particle multiplicities in Pb-Pb collisions at sNN−−−√ = 2.76 TeV using the ALICE detector at the CERN Large Hadron Collider (LHC) are presented in the pseudorapidity range |η|<0.8 and transverse momentum 0.2<pT<2.0 GeV/c. The amplitude of the fluctuations is expressed in terms of the variance normalized by the mean of the multiplicity distribution. The η and pT dependences of the fluctuations and their evolution with respect to collision centrality are investigated. The multiplicity fluctuations tend to decrease from peripheral to central collisions. The results are compared to those obtained from HIJING and AMPT Monte Carlo event generators as well as to experimental data at lower collision energies. Additionally, the measured multiplicity fluctuations are discussed in the context of the isothermal compressibility of the high-density strongly-interacting system formed in central Pb-Pb collisions.
The production of K∗(892)0 and ϕ(1020) mesons in proton-proton (pp) and lead-lead (Pb-Pb) collisions at sNN−−−√=5.02 TeV has been measured using the ALICE detector at the Large Hadron Collider (LHC). The transverse momentum (pT) distributions of K∗(892)0 and ϕ(1020) mesons have been measured at midrapidity (|y|<0.5) up to pT=20 GeV/c in inelastic pp collisions and for several Pb-Pb collision centralities. The collision centrality and collision energy dependence of the average transverse momenta agree with the radial flow scenario observed with stable hadrons, showing that the effect is stronger for more central collisions and higher collision energies. The K∗0/K ratio is found to be suppressed in Pb-Pb collisions relative to pp collisions: this indicates a loss of the measured K∗(892)0 signal due to rescattering of its decay products in the hadronic phase. In contrast, for the longer-lived ϕ(1020) mesons, no such suppression is observed. The nuclear modification factors (RAA) of K∗(892)0 and ϕ(1020) mesons are calculated using pp reference spectra at the same collision energy. In central Pb-Pb collisions for pT>8 GeV/c, the RAA values of K∗(892)0 and ϕ(1020) are below unity and observed to be similar to those of pions, kaons, and (anti)protons. The RAA values at high pT (>~8 GeV/c) for K∗(892)0 and ϕ(1020) mesons are in agreement within uncertainties for sNN−−−√=5.02 and 2.76 TeV.
Respiratory complex I in mitochondria and bacteria catalyzes the transfer of electrons from NADH to quinone (Q). The free energy available from the reaction is used to pump protons and to establish a membrane proton electrochemical gradient, which drives ATP synthesis. Even though several high-resolution structures of complex I have been resolved, how Q reduction is linked with proton pumping, remains unknown. Here, microsecond long molecular dynamics (MD) simulations were performed on Yarrowia lipolytica complex I structures where Q molecules have been resolved in the ~30 Å long Q tunnel. MD simulations of several different redox/protonation states of Q reveal the coupling between the Q dynamics and the restructuring of conserved loops and ion pairs. Oxidized quinone stabilizes towards the N2 FeS cluster, a binding mode not previously described in Yarrowia lipolytica complex I structures. On the other hand, reduced (and protonated) species tend to diffuse towards the Q binding sites closer to the tunnel entrance. Mechanistic and physiological relevance of these results are discussed.
Multiple resistance and pH adaptation (Mrp) cation/proton antiporters are essential for growth of a variety of halophilic and alkaliphilic bacteria under stress conditions. Mrp-type antiporters are closely related to the membrane domain of respiratory complex I. We determined the structure of the Mrp antiporter from Bacillus pseudofirmus by electron cryo-microscopy at 2.2 Å resolution. The structure resolves more than 99% of the sidechains of the seven membrane subunits MrpA to MrpG plus 360 water molecules, including ~70 in putative ion translocation pathways. Molecular dynamics simulations based on the high-resolution structure revealed details of the antiport mechanism. We find that switching the position of a histidine residue between three hydrated pathways in the MrpA subunit is critical for proton transfer that drives gated trans-membrane sodium translocation. Several lines of evidence indicate that the same histidine-switch mechanism operates in respiratory complex I.
Multiple resistance and pH adaptation (Mrp) cation/proton antiporters are essential for growth of a variety of halophilic and alkaliphilic bacteria under stress conditions. Mrp-type antiporters are closely related to the membrane domain of respiratory complex I. We determined the structure of the Mrp antiporter from Bacillus pseudofirmus by electron cryo-microscopy at 2.2 Å resolution. The structure resolves more than 99% of the sidechains of the seven membrane subunits MrpA to MrpG plus 360 water molecules, including ∼70 in putative ion translocation pathways. Molecular dynamics simulations based on the high-resolution structure revealed details of the antiport mechanism. We find that switching the position of a histidine residue between three hydrated pathways in the MrpA subunit is critical for proton transfer that drives gated transmembrane sodium translocation. Several lines of evidence indicate that the same histidine-switch mechanism operates in respiratory complex I.
Respiratory complex I in mitochondria and bacteria catalyzes the transfer of electrons from NADH to quinone (Q). The free energy available from the reaction is used to pump protons and to establish a membrane proton electrochemical gradient, which drives ATP synthesis. Even though several high-resolution structures of complex I have been resolved, how Q reduction is linked with proton pumping, remains unknown. Here, microsecond long molecular dynamics (MD) simulations were performed on Yarrowia lipolytica complex I structures where Q molecules have been resolved in the ~30 Å long Q tunnel. MD simulations of several different redox/protonation states of Q reveal the coupling between the Q dynamics and the restructuring of conserved loops and ion pairs. Oxidized quinone stabilizes towards the N2 FeS cluster, a binding mode not previously described in Yarrowia lipolytica complex I structures. On the other hand, reduced (and protonated) species tend to diffuse towards the Q binding sites closer to the tunnel entrance. Mechanistic and physiological relevance of these results are discussed.