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We have grown and characterized (110)-oriented YBa2Cu3O7−x (YBCO)/PrBa2(Cu0.8Ga0.2)3O7−x (PBCGO) bilayer and YBCO/PBCGO/YBCO trilayer heterostructures, which were deposited by pulsed laser deposition technique for the nanofabrication of (110)-oriented YBCO-based superconductor (S)/insulator (I)/superconductor (S) tunneling vertical geometry Josephson junction and other superconductor electronic devices. The structural properties of these heterostructures, investigated through various x-ray diffraction techniques (profile, x-ray reflectivity, pole figure, and reciprocal mapping), showed (110)-oriented epitaxial growth with a preferred c-axis-in-plane direction for all layers of the heterostructures. The atomic force microscopy measurement on the top surface of the heterostructures showed crack-free and pinhole-free, compact surface morphology with about a few nanometer root mean square roughness over the 5 × 5 μm2 region. The electrical resistivity measurements on the (110)-direction of the heterostructures showed superconducting critical temperature (Tc) values above 77 K and a very small proximity effect due to the interfacial contact of the superconducting YBCO layers with the PBCGO insulating layer. Raman spectroscopy measurements on the heterostructures showed the softening of the Ag-type Raman modes associated with the apical oxygen O(4) and O(2)-O(3)-in-phase vibrations compared to the stand-alone (110)-oriented PBCGO due to the residual stress and additional two Raman modes at ∼600 and ∼285 cm−1 frequencies due to the disorder at the Cu–O chain site of the PBCGO. The growth process and structural, electrical transport, and Raman spectroscopy characterization of (110)-oriented YBCO/PBCGO bilayer and YBCO/PBCGO/YBCO trilayer heterostructures are discussed in detail. 

Mitochondrial inner NEET (MiNT) and the outer mitochondrial membrane (OMM) mitoNEET (mNT) proteins belong to the NEET protein family. This family plays a key role in mitochondrial labile iron and reactive oxygen species (ROS) homeostasis. NEET proteins contain labile [2Fe-2S] clusters which can be transferred to apo-acceptor proteins. In eukaryotes, the biogenesis of [2Fe-2S] clusters occurs within the mitochondria by the iron–sulfur cluster (ISC) system; the clusters are then transferred to [2Fe-2S] proteins within the mitochondria or exported to cytosolic proteins and the cytosolic iron–sulfur cluster assembly (CIA) system. The last step of export of the [2Fe-2S] is not yet fully characterized. Here we show that MiNT interacts with voltage-dependent anion channel 1 (VDAC1), a major OMM protein that connects the intermembrane space with the cytosol and participates in regulating the levels of different ions including mitochondrial labile iron (mLI). We further show that VDAC1 is mediating the interaction between MiNT and mNT, in which MiNT transfers its [2Fe-2S] clusters from inside the mitochondria to mNT that is facing the cytosol. This MiNT–VDAC1–mNT interaction is shown both experimentally and by computational calculations. Additionally, we show that modifying MiNT expression in breast cancer cells affects the dynamics of mitochondrial structure and morphology, mitochondrial function, and breast cancer tumor growth. Our findings reveal a pathway for the transfer of [2Fe-2S] clusters, which are assembled inside the mitochondria, to the cytosol.