In iron-based superconductors, understanding the relation between superconductivity and electronic structure upon doping is crucial for exploring the pairing mechanism. Recently, it was found that, in iron selenide (FeSe), enhanced superconductivity ( of more than 40 K) can be achieved via electron doping, with the Fermi surface only comprising M-centered electron pockets. By using surface K dosing, scanning tunneling microscopy/spectroscopy, and angle-resolved photoemission spectroscopy, we studied the electronic structure and superconductivity of (LiFeOH)FeSe in the deep electron-doped regime. We find that a Γ-centered electron band, which originally lies above the Fermi level (), can be continuously tuned to cross and contribute a new electron pocket at Γ. When this Lifshitz transition occurs, the superconductivity in the M-centered electron pocket is slightly suppressed, and a possible superconducting gap with a small size (up to ~5 meV) and a dome-like doping dependence is observed on the new Γ electron pocket. Upon further K dosing, the system eventually evolves into an insulating state. Our findings provide new clues to understand superconductivity versus Fermi surface topology and the correlation effect in FeSe-based superconductors.
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http://dx.doi.org/10.1126/sciadv.1603238 | DOI Listing |
Sci Adv
January 2025
National Laboratory of Solid State Microstructures, Jiangsu Key Laboratory of Artificial Functional Materials, College of Engineering and Applied Sciences, Nanjing University, Nanjing 210093, China.
Revealing the momentum-resolved electronic structure of infinite-layer nickelates is essential for understanding this class of unconventional superconductors but has been hindered by the formidable challenges in improving the sample quality. In this work, we report the angle-resolved photoemission spectroscopy of superconducting LaSrNiO films prepared by molecular beam epitaxy and in situ atomic-hydrogen reduction. The measured Fermi topology closely matches theoretical calculations, showing a large Ni [Formula: see text]-derived Fermi sheet that evolves from hole-like to electron-like along and a three-dimensional (3D) electron pocket centered at the Brillouin zone corner.
View Article and Find Full Text PDFAdv Sci (Weinh)
January 2025
Université Paris-Saclay, CNRS, Institut de Chimie Moléculaire et des Matériaux d'Orsay, Orsay, 91400, France.
To efficiently capture, activate, and transform small molecules, metalloenzymes have evolved to integrate a well-organized pocket around the active metal center. Within this cavity, second coordination sphere functionalities are precisely positioned to optimize the rate, selectivity, and energy cost of catalytic reactions. Inspired by this strategy, an artificial distal pocket defined by a preorganized 3D strap is introduced on an iron-porphyrin catalyst (sc-Fe) for the CO-to-CO electrocatalytic reduction.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5, Kashiwanoha, Kashiwa, Chiba 277-8562, Japan.
U6 snRNA (small nuclear ribonucleic acid) is a ribozyme that catalyzes pre-messenger RNA (pre-mRNA) splicing and undergoes epitranscriptomic modifications. After transcription, the 3'-end of U6 snRNA is oligo-uridylylated by the multi-domain terminal uridylyltransferase (TUTase), TUT1. The 3'- oligo-uridylylated tail of U6 snRNA is crucial for U4/U6 di-snRNP (small nuclear ribonucleoprotein) formation and pre-mRNA splicing.
View Article and Find Full Text PDFUnlabelled: Myosin-IC (myo1c) is a class-I myosin that supports transport and remodeling of the plasma membrane and membrane-bound vesicles. Like other members of the myosin family, its biochemical kinetics are altered in response to changes in mechanical loads that resist the power stroke. However, myo1c is unique in that the primary force-sensitive kinetic transition is the isomerization that follows ATP binding, not ADP release as in other slow myosins.
View Article and Find Full Text PDFNat Commun
January 2025
Laboratory of Biological Electron Microscopy, IPHYS, SB, EPFL, and Dept. Fundamental Microbiology, Faculty of Biology and Medicine, UNIL, Cubotron, Rt. de la Sorge, Lausanne, Switzerland.
Transient receptor potential (TRP) melastatin 4 (TRPM4) protein is a calcium-activated monovalent cation channel associated with various genetic and cardiovascular disorders. The anthranilic acid derivative NBA is a potent and specific TRPM4 inhibitor, but its binding site in TRPM4 has been unknown, although this information is crucial for drug development targeting TRPM4. We determine three cryo-EM structures of full-length human TRPM4 embedded in native lipid nanodiscs without inhibitor, bound to NBA, and an anthranilic acid derivative, IBA.
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