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1. 1,8-Bis(borylamido)naphthalene Complexes of Lithium and Zinc(II) Including a Zinc(II) Isocyanide Adduct: 1,8-Bis(borylamido)naphthalene Complexes of Lithium and Zinc(II) Including a Zinc(II) Isocyanide Adduct

   https://doi.org/10.1002/ejic.201701099  

   Wang, Guocang ; Dias, H. V. ( December 2017 , European Journal of Inorganic Chemistry)
2. Reversible Zinc Electrodeposition at −60 °C Using a Deep Eutectic Electrolyte for Low-Temperature Zinc Metal Batteries

   https://doi.org/10.1021/acs.jpclett.3c00150  

   Hawkins, Brendan E. ; Schoetz, Theresa ; Gordon, Leo W. ; KT, Surabh ; Wang, Jonah ; Messinger, Robert J. ( February 2023 , The Journal of Physical Chemistry Letters)
3. Length dependence thermal conductivity of zinc selenide (ZnSe) and zinc telluride (ZnTe) – a combined first principles and frequency domain thermoreflectance (FDTR) study

   https://doi.org/10.1039/d2cp03612f  

   Muthaiah, Rajmohan ; Annam, Roshan Sameer ; Tarannum, Fatema ; Gupta, Ashish Kumar ; Garg, Jivtesh ; Arafin, Shamsul ( December 2022 , Physical Chemistry Chemical Physics)

   In this study, we report the length dependence of thermal conductivity ( k ) of zinc blende-structured Zinc Selenide (ZnSe) and Zinc Telluride (ZnTe) for length scales between 10 nm and 10 μm using first-principles computations, based on density-functional theory. The k value of ZnSe is computed to decrease significantly from 22.9 W m −1 K −1 to 1.8 W m −1 K −1 as the length scale is diminished from 10 μm to 10 nm. The k value of ZnTe is also observed to decrease from 12.6 W m −1 K −1 to 1.2 W m −1 K −1 for the same decrease in length. We also measured the k of bulk ZnSe and ZnTe using the Frequency Domain Thermoreflectance (FDTR) technique and observed a good agreement between the FDTR measurements and first principles calculations for bulk ZnSe and ZnTe. Understanding the thermal conductivity reduction at the nanometer length scale provides an avenue to incorporate nanostructured ZnSe and ZnTe for thermoelectric applications. 

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4. Adsorption of Carbon Dioxide, Methane, and Nitrogen Gases onto ZIF Compounds with Zinc, Cobalt, and Zinc/Cobalt Metal Centers

   https://doi.org/10.1155/2019/6130152  

   Awadallah-F, Ahmed ; Hillman, Febrian ; Al-Muhtaseb, Shaheen A. ; Jeong, Hae-Kwon ( December 2019 , Journal of Nanomaterials)

   null (Ed.)

   ZIF-8, Co-ZIF-8, and Zn/Co-ZIF-8 are utilized in adsorbing nitrogen (N 2 ), methane (CH 4 ), and carbon dioxide (CO 2 ) gases at temperatures between 25 and 55°C and pressures up to ~1 MPa. Equilibrium adsorption isotherms and adsorption kinetics are studied. The dual-site Langmuir equation is employed to correlate the nonisothermal adsorption equilibrium behavior. Generally, N 2 showed the lowest equilibrium adsorption quantity on the three samples, whereas CO 2 showed the highest equilibrium adsorption capacity. Amid the ZIF samples, the biggest adsorption quantities of N 2 and CH 4 were onto Zn/Co-ZIF-8, whereas the highest adsorption quantity of CO 2 was on ZIF-8. The isosteric heats of adsorbing these gases on ZIF-8, Co-ZIF-8, and Zn/Co-ZIF-8 were examined. Moreover, the overall mass transfer coefficients of adsorption at different temperatures were investigated. 

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5. Synaptic zinc inhibition of NMDA receptors depends on the association of GluN2A with the zinc transporter ZnT1

   https://doi.org/10.1126/sciadv.abb1515  

   Krall, Rebecca F. ; Moutal, Aubin ; Phillips, Matthew B. ; Asraf, Hila ; Johnson, Jon W. ; Khanna, Rajesh ; Hershfinkel, Michal ; Aizenman, Elias ; Tzounopoulos, Thanos ( July 2020 , Science Advances)

   The NMDA receptor (NMDAR) is inhibited by synaptically released zinc. This inhibition is thought to be the result of zinc diffusion across the synaptic cleft and subsequent binding to the extracellular domain of the NMDAR. However, this model fails to incorporate the observed association of the highly zinc-sensitive NMDAR subunit GluN2A with the postsynaptic zinc transporter ZnT1, which moves intracellular zinc to the extracellular space. Here, we report that disruption of ZnT1-GluN2A association by a cell-permeant peptide strongly reduced NMDAR inhibition by synaptic zinc in mouse dorsal cochlear nucleus synapses. Moreover, synaptic zinc inhibition of NMDARs required postsynaptic intracellular zinc, suggesting that cytoplasmic zinc is transported by ZnT1 to the extracellular space in close proximity to the NMDAR. These results challenge a decades-old dogma on how zinc inhibits synaptic NMDARs and demonstrate that presynaptic release and a postsynaptic transporter organize zinc into distinct microdomains to modulate NMDAR neurotransmission. 

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