@article{8910,
  abstract     = {A semiconducting nanowire fully wrapped by a superconducting shell has been proposed as a platform for obtaining Majorana modes at small magnetic fields. In this study, we demonstrate that the appearance of subgap states in such structures is actually governed by the junction region in tunneling spectroscopy measurements and not the full-shell nanowire itself. Short tunneling regions never show subgap states, whereas longer junctions always do. This can be understood in terms of quantum dots forming in the junction and hosting Andreev levels in the Yu-Shiba-Rusinov regime. The intricate magnetic field dependence of the Andreev levels, through both the Zeeman and Little-Parks effects, may result in robust zero-bias peaks—features that could be easily misinterpreted as originating from Majorana zero modes but are unrelated to topological superconductivity.},
  author       = {Valentini, Marco and Peñaranda, Fernando and Hofmann, Andrea C and Brauns, Matthias and Hauschild, Robert and Krogstrup, Peter and San-Jose, Pablo and Prada, Elsa and Aguado, Ramón and Katsaros, Georgios},
  issn         = {10959203},
  journal      = {Science},
  number       = {6550},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Nontopological zero-bias peaks in full-shell nanowires induced by flux-tunable Andreev states}},
  doi          = {10.1126/science.abf1513},
  volume       = {373},
  year         = {2021},
}

@article{8737,
  abstract     = {Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different conditions, including turnover, at resolutions up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally define the proton translocation pathways. Quinone binds at three positions along the quinone cavity, as does the inhibitor rotenone that also binds within subunit ND4. Dramatic conformational changes around the quinone cavity couple the redox reaction to proton translocation during open-to-closed state transitions of the enzyme. In the induced deactive state, the open conformation is arrested by the ND6 subunit. We propose a detailed molecular coupling mechanism of complex I, which is an unexpected combination of conformational changes and electrostatic interactions.},
  author       = {Kampjut, Domen and Sazanov, Leonid A},
  issn         = {10959203},
  journal      = {Science},
  number       = {6516},
  publisher    = {American Association for the Advancement of Science},
  title        = {{The coupling mechanism of mammalian respiratory complex I}},
  doi          = {10.1126/science.abc4209},
  volume       = {370},
  year         = {2020},
}