All Publications

  • Field-Responsive Dynamic Monolayer Regulated Interphase for Enhanced Lithium Metal Batteries. Journal of the American Chemical Society Zhang, E., Holoubek, J., Lyu, H., Li, Y., Florian, J., Shuchi, S. B., Lee, J. K., Michalek, L., Chen, T., Chen, Z., Choi, I. R., Guo, X., Mondonico, L., Cui, Y., Bao, Z. 2026

    Abstract

    Lithium metal batteries offer high energy density but suffer from persistent interphase instability, where continuous corrosion, solid electrolyte interphase (SEI) growth and poor lithium deposition morphology remain key barriers to long cycle and calendar life. Here, we introduce a novel concept of dynamic monolayers on Li metal anodes, consisting of electric field-responsive molecules that assemble into packed, structured layers at the lithium interphase under an applied voltage. We employed electrochemical quartz crystal microbalance with dissipation monitoring for in situ verification of the field responsiveness and packing behavior of these molecules. Dynamic monolayers with stronger packing are found to promote more inorganic-rich SEI and chunkier lithium growth, as directly observed by cryogenic X-ray photoelectron spectroscopy and operando optical microscopy. Together, these interfacial improvements translate into enhanced Coulombic Efficiency, reduced overpotential, and improved long-term cycling stability across Li||Cu, Li||Li, ultrathin lithium (20 mum) and anode-free NMC811 configurations. Dynamic monolayers potentially provide a broadly applicable approach for tackling interfacial challenges across a range of alkali metal battery systems.

    View details for DOI 10.1021/jacs.5c19365

    View details for PubMedID 41649298

  • Simply Fabricatable Reference Electrode for Studying Li Metal Interfaces <i>Operando</i> ACS ENERGY LETTERS Florian, J., Lyu, H., Mondonico, L., Zhao, Y., Lee, J. K. J., Musgrove, A. L., Cui, Y., Sacci, R. L., Bao, Z. 2026

    View details for DOI 10.1021/acsenergylett.5c03496

    View details for Web of Science ID 001659662500001

  • Mesh-like structure integrated core-shell-shell nanocomposites for enhanced stability and performance in carbon capture. Nature communications Yang, S., Mao, H., Dun, C., Liu, J., Hou, K., Cai, A., Wang, J., Lee, J. K., Li, D., Lyu, H., Chen, Z., Lv, X., Zhuang, H., Xu, X., Zheng, X., Ren, G., Reimer, J. A., Cui, Y., Urban, J. J. 2025; 16 (1): 10526

    Abstract

    Carbon capture is essential for mitigating climate change, yet most sorbents struggle to combine high capacity with chemical stability. Here we report core-shell-shell (CSS) nanocomposites that integrate adsorption efficiency with exceptional robustness. The design couples a metal-organic framework (MOF) core, which enriches local CO2 concentration, with a polyamine shell that is reorganized into a porous, ordered network through entanglement with an outer covalent organic framework (COF) shell. This hierarchical architecture enables dual amine functionalization via sequential "click" and Schiff-base reactions, achieving a CO2 uptake of 3.4 mmol g-1 at 1 bar. The COF outer layer also acts as a protective barrier, suppressing humidity interference and doubling cycling stability under simulated flue gas. Remarkably, the nanocomposites maintain structural integrity after one week in strongly acidic (3 M HNO3) or basic (NaOH, pH=14) environments, underscoring their chemical resilience. By uniting high capacity, cycling durability, and environmental tolerance, this CSS strategy offers a versatile platform for next-generation carbon capture materials.

    View details for DOI 10.1038/s41467-025-65531-3

    View details for PubMedID 41298365

    View details for PubMedCentralID PMC12658231

  • Resolving three-dimensional nanoscale heterogeneities in lithium metal batteries with cryoelectron tomography MATTER Zhang, Z., Lee, J. K. J., Li, Y., Zhou, W., Wu, G., Lyu, H., Wan, J., Chen, H., Huang, W., Ye, Y., Schmid, M. F., Cui, Y., Chiu, W. 2025; 8 (7)

    View details for DOI 10.1016/j.matt.2025.102266

    View details for Web of Science ID 001532637500008

  • Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing SCIENCE Liu, S., Wang, H., Li, X., Zhang, F., Lee, J. K. J., Li, Z., Yu, C., Hu, J. J., Zhao, X., Suematsu, T., Alvarez-Cabrera, A. L., Liu, Q., Zhang, L., Huang, L., Aphasizheva, I., Aphasizhev, R., Zhou, Z. 2023; 381 (6653): 43-+

    Abstract

    In Trypanosoma brucei, the editosome, composed of RNA-editing substrate-binding complex (RESC) and RNA-editing catalytic complex (RECC), orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs (mRNAs). The mechanism of information transfer from gRNA to mRNA is unclear owing to a lack of high-resolution structures for these complexes. With cryo-electron microscopy and functional studies, we have captured gRNA-stabilizing RESC-A and gRNA-mRNA-binding RESC-B and RESC-C particles. RESC-A sequesters gRNA termini, thus promoting hairpin formation and blocking mRNA access. The conversion of RESC-A into RESC-B or -C unfolds gRNA and allows mRNA selection. The ensuing gRNA-mRNA duplex protrudes from RESC-B, likely exposing editing sites to RECC-catalyzed cleavage, uridine insertion or deletion, and ligation. Our work reveals a remodeling event facilitating gRNA-mRNA hybridization and assembly of a macromolecular substrate for the editosome's catalytic modality.

    View details for DOI 10.1126/science.adg4725

    View details for Web of Science ID 001030999200003

    View details for PubMedID 37410820

    View details for PubMedCentralID PMC10704856

  • CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics JOURNAL OF STRUCTURAL BIOLOGY-X Lee, J. K. J., Liu, Y., Hu, J. J., Aphasizheva, I., Aphasizhev, R., Zhou, Z. 2023; 7: 100088

    Abstract

    Propionyl-CoA carboxylase (PCC) is a multienzyme complex consisting of up to six α-subunits and six β-subunits. Belonging to a metabolic pathway converging on the citric acid cycle, it is present in most forms of life and irregularities in its assembly lead to serious illness in humans, known as propionic acidemia. Here, we report the cryogenic electron microscopy (cryoEM) structures and assembly of different oligomeric isomers of endogenous PCC from the parasitic protozoan Leishmania tarentolae (LtPCC). These structures and their statistical distribution reveal the mechanics of PCC assembly and disassembly at equilibrium. We show that, in solution, endogenous LtPCC β-subunits form stable homohexamers, to which different numbers of α-subunits attach. Sorting LtPCC particles into seven classes (i.e., oligomeric formulae α0β6, α1β6, α2β6, α3β6, α4β6, α5β6, α6β6) enables formulation of a model for PCC assembly. Our results suggest how multimerization regulates PCC enzymatic activity and showcase the utility of cryoEM in revealing the statistical mechanics of reaction pathways.

    View details for DOI 10.1016/j.yjsbx.2023.100088

    View details for Web of Science ID 001113614100001

    View details for PubMedID 37128595

    View details for PubMedCentralID PMC10148081

  • Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase STRUCTURE Hu, J. J., Lee, J. K. J., Liu, Y., Yu, C., Huang, L., Aphasizheva, I., Aphasizhev, R., Zhou, Z. 2023; 31 (1): 100-+

    Abstract

    3-methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent mitochondrial enzyme necessary for leucine catabolism in most organisms. While the crystal structure of recombinant bacterial MCC has been characterized, the structure and potential polymerization of native MCC remain elusive. Here, we discovered that native MCC from Leishmania tarentolae (LtMCC) forms filaments, and determined the structures of different filament regions at 3.4, 3.9, and 7.3 Å resolution using cryoEM. α6β6 LtMCCs assemble in a twisted-stacks architecture, manifesting as supramolecular rods up to 400 nm. Filamentous LtMCCs bind biotin non-covalently and lack coenzyme A. Filaments elongate by stacking α6β6 LtMCCs onto the exterior α-trimer of the terminal LtMCC. This stacking immobilizes the biotin carboxylase domains, sequestering the enzyme in an inactive state. Our results support a new model for LtMCC catalysis, termed the dual-swinging-domains model, and cast new light on the function of polymerization in the carboxylase superfamily and beyond.

    View details for DOI 10.1016/j.str.2022.11.015

    View details for Web of Science ID 000932407000001

    View details for PubMedID 36543169

    View details for PubMedCentralID PMC9825669