JACS AuPub Date : 2025-05-15DOI: 10.1021/jacsau.5c0030710.1021/jacsau.5c00307
Donggyu Lee, Seungyun Lee, Jinhyeok Jang, Jun Young Oh, Younghun Kim, Sam-Jong Choi, Yun Ho Kim* and Jihyun Kim*,
{"title":"Insulator-Based Dielectrophoresis for Purifying Semiconductor Industry-Compatible Chemicals with Trace Nanoparticles","authors":"Donggyu Lee, Seungyun Lee, Jinhyeok Jang, Jun Young Oh, Younghun Kim, Sam-Jong Choi, Yun Ho Kim* and Jihyun Kim*, ","doi":"10.1021/jacsau.5c0030710.1021/jacsau.5c00307","DOIUrl":"https://doi.org/10.1021/jacsau.5c00307https://doi.org/10.1021/jacsau.5c00307","url":null,"abstract":"<p >As semiconductor scaling advances below 2–3 nm dimensions, precise control of nanoscale impurities becomes crucial for maintaining device performance and production yield. Conventional purification methods, such as distillation and filtration, are ineffective in removing nanoparticles smaller than 10 nm. This study investigates insulator-based dielectrophoresis (iDEP) for efficient removal of silica nanoparticles from semiconductor processing chemicals. Interdigitated electrode patterns fabricated on sapphire substrates were employed to generate high electric field gradients, facilitating nanoparticle aggregation. A 20 nm-thick aluminum oxide passivation layer was deposited via atomic layer deposition to prevent electrode degradation. Finite element method simulations confirmed that the strong electric field gradient necessary for nanoparticle aggregation was generated at the electrode edges. The optimal frequency for nanoparticle aggregation was determined using the Clausius–Mossotti factor, and large-scale iDEP experiments demonstrated a 41.3% reduction in Si concentration in deionized water and a 23.4% reduction in 2% nitric acid after 12 purification cycles. This method effectively removes the nanoparticles that are difficult to eliminate using conventional techniques, enhancing the purity of semiconductor processing chemicals. The study demonstrates iDEP’s scalability, high throughput, and reliability for industrial applications, offering a promising solution for meeting purity standards in semiconductor fabrication.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2342–2349 2342–2349"},"PeriodicalIF":8.5,"publicationDate":"2025-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00307","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144133902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-15DOI: 10.1021/jacsau.5c0022410.1021/jacsau.5c00224
Ruslan Gibadullin*, Óscar Suárez, Foivos S. Lazaris, Naiara Gutiez, Estibaliz Atondo, Sarai Araujo-Aris, Ander Eguskiza, Jiani Niu, Ariel J. Kuhn, Ana S. Grosso, Héctor Rodriguez, Fayna García-Martín, Filipa Marcelo, Tanausú Santos, Alberto Avenoza, Jesús H. Busto, Jesús M. Peregrina, Samuel H. Gellman, Juan Anguita*, Roberto Fiammengo* and Francisco Corzana*,
{"title":"Enhancing Cancer Vaccine Efficacy: Backbone Modification with β-Amino Acids Alters the Stability and Immunogenicity of MUC1-Derived Glycopeptide Formulations","authors":"Ruslan Gibadullin*, Óscar Suárez, Foivos S. Lazaris, Naiara Gutiez, Estibaliz Atondo, Sarai Araujo-Aris, Ander Eguskiza, Jiani Niu, Ariel J. Kuhn, Ana S. Grosso, Héctor Rodriguez, Fayna García-Martín, Filipa Marcelo, Tanausú Santos, Alberto Avenoza, Jesús H. Busto, Jesús M. Peregrina, Samuel H. Gellman, Juan Anguita*, Roberto Fiammengo* and Francisco Corzana*, ","doi":"10.1021/jacsau.5c0022410.1021/jacsau.5c00224","DOIUrl":"https://doi.org/10.1021/jacsau.5c00224https://doi.org/10.1021/jacsau.5c00224","url":null,"abstract":"<p >Glycopeptides derived from the mucin-1 (MUC1) glycoprotein hold significant promise as cancer vaccine candidates, but their clinical utility is limited by proteolytic degradation and the poor bioavailability of <span>L</span>-α-amino acid–based peptides. In this study, we demonstrate that substitution of multiple α-amino acids with homologous β-amino acids (same side chain, but extended backbone) in <i>O</i>-glycosylated MUC1 derivatives significantly enhances their proteolytic stability. We further show that α-to-β substitutions within the most immunogenic epitope of MUC1 impede binding to an anti-MUC1 antibody, while substitutions outside the same epitope preserve antibody recognition. Structural investigations using circular dichroism, NMR spectroscopy, and molecular dynamics simulations reveal that the strongest α/β-peptide binders retain native-like conformations in the epitope region, both in their unbound state and when bound to the anti-MUC1 antibody. Conjugation of these high-affinity α/β-peptide analogs to gold nanoparticles induces robust immune responses in mice comparable to that of the native glycopeptide. Additionally, these α/β-analogs elicit elevated levels of the cytokine IFNγ, one of the key proteins for tumor cell elimination, surpassing levels produced by the native MUC1 glycopeptide. In contrast, a low-affinity α/β-analogue with lower proteolytic stability produces minimal cytokine responses, underscoring the critical role of these biochemical properties in vaccine efficacy. Collectively, our findings highlight that α-to-β modifications in the peptide backbone offer an effective strategy for developing biostable, highly immunogenic glycopeptide-based cancer vaccines, exemplifying the power of structure-based rational design in advancing next-generation vaccines.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2270–2284 2270–2284"},"PeriodicalIF":8.5,"publicationDate":"2025-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00224","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144134027","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Robust Accessibility of Addressable Sites in Defective DNA Origami","authors":"Zheze Dai, Xiaodong Xie, Xiaoliang Chen, Hui Lv, Yao Xie, Yongjun Liu, Fei Wang, Mingqiang Li, Chunhai Fan* and Qian Li*, ","doi":"10.1021/jacsau.5c0020610.1021/jacsau.5c00206","DOIUrl":"https://doi.org/10.1021/jacsau.5c00206https://doi.org/10.1021/jacsau.5c00206","url":null,"abstract":"<p >Owing to its unique programmability and addressability, DNA origami-based nanofabrication has been widely utilized in fields such as nanomedicine and nanophotonics. The accessibility of addressable sites on DNA origami structures is crucial for their use as nanofabrication platforms. In this study, we systematically investigated the impact of structural defects on accessibility using a classic six-helix bundle (6HB) DNA origami and two variants with subsets of DNA staple strands deleted, introducing programmable defects in 6HB nanostructures. DNA point accumulation for imaging in nanoscale topography super-resolution microscopy was employed to monitor hybridization and dehybridization at each addressable site and analyze corresponding localizations and kinetics. Statistical analysis revealed that addressable sites on 6HB nanostructures retained significant accessibility robustness despite structural defects, which was further supported by molecular dynamics simulations. These results provide valuable insights into the design principles and applications of DNA origami.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2237–2245 2237–2245"},"PeriodicalIF":8.5,"publicationDate":"2025-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00206","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144133838","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-12DOI: 10.1021/jacsau.5c0024510.1021/jacsau.5c00245
Paula L. Jordan, Heiner N. Raum, Stefan Gröger and Ulrich Weininger*,
{"title":"Protonation Kinetics in Proteins at Basic pH Determined by pH-Dependent NMR Relaxation Reveal the Entire Relationship between Kinetics and pKa Values","authors":"Paula L. Jordan, Heiner N. Raum, Stefan Gröger and Ulrich Weininger*, ","doi":"10.1021/jacsau.5c0024510.1021/jacsau.5c00245","DOIUrl":"https://doi.org/10.1021/jacsau.5c00245https://doi.org/10.1021/jacsau.5c00245","url":null,"abstract":"<p >Ionizable amino acid side chains in proteins undergo constant protonation and deprotonation reactions. These proton exchange dynamics are a fundamental feature of proteins and their electrostatic character, as well as the basis for many biological processes, such as general acid–base enzyme catalysis. Such dynamics have been measured in a site-specific way for aspartates, glutamates, and histidines by pH-dependent NMR relaxation experiments. Linear free-energy relationships between kinetic and thermodynamic parameters have been established that allow the description of proton-mediated proton exchange at low to neutral pH. Here, we complement the picture by determining the proton exchange kinetics of lysine and tyrosine side chains at basic pH. They display matching linear free-energy relationships that enable the description of hydroxide-mediated proton exchange at high pH. The underlying maximal second-order rate constants are approximately a factor of 40 higher for hydronium association compared to hydroxide dissociation. These combined findings provide a general framework for describing protonation kinetics, allowing for the prediction of protonation and deprotonation rate constants for ionizable groups with all possible p<i>K</i><sub>a</sub> values across the entire pH range.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2334–2341 2334–2341"},"PeriodicalIF":8.5,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00245","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144133991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-12DOI: 10.1021/jacsau.5c0005810.1021/jacsau.5c00058
Weiming Lin, Tao Ding, Die He, Nan Zhang, Haodong Li, Wenjian Luo, Zhongxia Wei, Min Ke, Sisi Jia*, Chunhai Fan and Le Liang*,
{"title":"DNA Logic-Integrated Quantum Nanosensor for MicroRNA Diagnostics","authors":"Weiming Lin, Tao Ding, Die He, Nan Zhang, Haodong Li, Wenjian Luo, Zhongxia Wei, Min Ke, Sisi Jia*, Chunhai Fan and Le Liang*, ","doi":"10.1021/jacsau.5c0005810.1021/jacsau.5c00058","DOIUrl":"https://doi.org/10.1021/jacsau.5c00058https://doi.org/10.1021/jacsau.5c00058","url":null,"abstract":"<p >Nanodiamonds (NDs) with nitrogen-vacancy (NV) centers are emerging as powerful quantum nanosensors (QNs) in biomedical applications due to their exceptional sensitivity. However, achieving optimal diagnostics performance necessitates both high sensitivity and selectivity; especially in practical biomedical settings, it remains challenging for QNs to provide quantitative analyses when multiple analytes are present. Here, we present a biosensing platform that integrates DNA logic gates (DLGs) with spin-based quantum sensing, termed DLG-QN for ultrasensitive and ultraselective diagnostics. Utilizing an AND DLG, both NDs and magnetic beads (MBs) are functionalized with hairpin DNA strands. In the presence of both miRNA-21 and miRNA-155─key biomarkers overexpressed in cancer─the hairpin DNAs undergo conformational changes that facilitate DNA-guided self-assembly of NDs and MBs, enriching the target signal. Resonant microwave modulation of ND fluorescence emission allows for high signal-to-noise ratio (SNR) detection by separating the signal from background fluorescence via spin-enhanced analysis. This platform demonstrated ultrasensitive and ultraselective detection of miRNA-21 and miRNA-155 with a limit of detection of 19.8 fM, highlighting its potential as a general biosensing strategy for precision diagnostics involving multiple biomarkers.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2123–2134 2123–2134"},"PeriodicalIF":8.5,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00058","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144133969","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-09DOI: 10.1021/jacsau.5c0039010.1021/jacsau.5c00390
Medha Aggarwal, Ranit Banerjee, Neal Hickey and Partha Sarathi Mukherjee*,
{"title":"Formation of a Pd16 Molecular Basket Architecture of Reduced Symmetry and Angular Deviation in a Fluorenone Scaffold to Govern the Host–Guest Chemistry of Pd6 Trifacial Tubes","authors":"Medha Aggarwal, Ranit Banerjee, Neal Hickey and Partha Sarathi Mukherjee*, ","doi":"10.1021/jacsau.5c0039010.1021/jacsau.5c00390","DOIUrl":"https://doi.org/10.1021/jacsau.5c00390https://doi.org/10.1021/jacsau.5c00390","url":null,"abstract":"<p >The employment of flexible ligands with significant conformational freedom in coordination-driven self-assembly enables the formation of unique and intricate structures. In this study, the self-assembly of such a fluorenone-appended ligand (<b>L1</b>) with a sterically demanding acceptor, [Pd(tmed)(ONO<sub>2</sub>)<sub>2</sub>] (<b>M1</b>), generated a new and unique molecular basket architecture, (<b>M1</b>)<b><sub>16</sub></b>(<b>L1</b>)<b><sub>8</sub></b> (<b>B</b>), featuring a large hollow cavity. <b>B</b> possesses an unusual twisted architecture of low symmetry, consisting of 16 Pd(II) centers arranged as four tetrahedra connected by eight flexible ligands, representing a structurally complex system reminiscent of biological architectures. Designing such entropically disfavored, large architectures of reduced symmetry is challenging but desirable, since they can act as ideal models to study complicated natural systems. The host–guest property of supramolecular hosts is governed by the confined cavities and noncovalent interactions, which are dictated by the angular disposition of ligand coordination sites. To explore this, the fluorenone scaffold was used to synthesize two other tetradentate ligands (<b>L2</b> and <b>L3</b>) that differed in the spatial distributions of their coordination vectors. The self-assembly of these ligands with [Pd(en)(ONO<sub>2</sub>)<sub>2</sub>] (<b>M2</b>) resulted in the formation of water-soluble (<b>M2</b>)<b><sub>6</sub></b>(<b>L1</b>/<b>L2</b>/<b>L3</b>)<b><sub>3</sub></b> trifacial tubes of different geometries with varying internal cavity dimensions. These angular variations further altered the orientation of the fluorenone carbonyl groups within the cavities, thereby modulating their guest binding abilities and highlighting the importance of tailoring supramolecular hosts for specific guest binding.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2368–2378 2368–2378"},"PeriodicalIF":8.5,"publicationDate":"2025-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00390","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144134045","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-09DOI: 10.1021/jacsau.5c0014610.1021/jacsau.5c00146
Yu-Kai Cheng, Hsing-Hui Chu, Ning-Jun Yang and Yei-Chen Lai*,
{"title":"Decoupling Global and Local Structural Changes in Self-aminoacylating Ribozymes Reveals the Critical Role of Local Structural Dynamics in Ribozyme Activity","authors":"Yu-Kai Cheng, Hsing-Hui Chu, Ning-Jun Yang and Yei-Chen Lai*, ","doi":"10.1021/jacsau.5c0014610.1021/jacsau.5c00146","DOIUrl":"https://doi.org/10.1021/jacsau.5c00146https://doi.org/10.1021/jacsau.5c00146","url":null,"abstract":"<p >Self-aminoacylating ribozymes catalyze the attachment of amino acids to RNA, serving as pivotal models to investigate the catalytic roles of RNA in prebiotic evolution. In this study, we investigated how divalent metal ions (Mg<sup>2+</sup> and Ca<sup>2+</sup>) modulate local and global structures in two such ribozymes, S-1A.1-a and S-2.1-a, using 4-cyanotryptophan (4CNW) fluorescence and native gel electrophoresis. By tracking 4CNW fluorescence changes at varying concentrations of Mg<sup>2+</sup> and Ca<sup>2+</sup> and temperatures, we determined how these ions influence the catalytic sites and overall conformations of the ribozymes. Our findings reveal that Mg<sup>2+</sup> specifically binds to S-1A.1-a at low concentrations, stabilizing the local structure around the aminoacylation site and causing the site to become more buried, which is essential for catalytic activity. Although higher Mg<sup>2+</sup> and Ca<sup>2+</sup> concentrations induce global structural rearrangements, these shifts have minimal impact on the local environment of the aminoacylation site, underscoring the dominance of local structural stability in sustaining ribozyme function. In contrast, the activity of S-2.1-a effectively adapts to both Mg<sup>2+</sup> and Ca<sup>2+</sup>, and its fluorescence results indicate a more solvent-exposed aminoacylation site. Overall, these data highlight that local structural changes in the ribozyme’s catalytic core are more critical for its function than global conformational shifts. Our study highlights the importance of local environmental changes in ion-dependent ribozyme catalysis and provides insights into the molecular mechanisms of self-aminoacylating ribozymes.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2172–2185 2172–2185"},"PeriodicalIF":8.5,"publicationDate":"2025-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00146","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144134007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-08DOI: 10.1021/jacsau.5c0035210.1021/jacsau.5c00352
Roushan Prakash Singh, and , Neal P. Mankad*,
{"title":"Molecular Design of Al(II) Intermediates for Small Molecule Activation","authors":"Roushan Prakash Singh, and , Neal P. Mankad*, ","doi":"10.1021/jacsau.5c0035210.1021/jacsau.5c00352","DOIUrl":"https://doi.org/10.1021/jacsau.5c00352https://doi.org/10.1021/jacsau.5c00352","url":null,"abstract":"<p >Promoting societally important small molecule activation processes with earth-abundant metals is foundational for a sustainable chemistry future. In this context, mapping new reaction pathways that would enable abundant main-group elements to mimic the behaviors of <i>d</i>- and <i>f</i>-block elements is facilitated by exploring unusual oxidation states. The most abundant metal on earth, aluminum, has been well studied in the Lewis acidic +III and Lewis basic +I oxidation states but rarely in the potentially biphilic +II oxidation state until recently, when a renaissance of Al(II) chemistry emerged from a range of research groups. In this Perspective, we review the chemistry of mononuclear Al radicals, including both Al-centered radicals (i.e., Al(II) compounds) and redox non-innocent systems (i.e., formally Al(II) species that are physically Al(III) with ligand-centered radicals), with an emphasis on small molecule reactivity. We also provide a meta-analysis of the Al(II) literature to summarize how different design strategies (e.g., redox non-innocence, strained coordination geometries) have been shown to impart biphilic character to Al radicals and tune their behavior, thus allowing Al radicals to mimic the chemistry of certain <i>d</i>- and <i>f</i>-block metal ions such as Ti(III) and Sm(II). We expect these molecular design concepts to inform future Al(II) studies as the chemistry of this unusual oxidation state of Al continues to grow.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2076–2088 2076–2088"},"PeriodicalIF":8.5,"publicationDate":"2025-05-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00352","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144133919","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
JACS AuPub Date : 2025-05-07DOI: 10.1021/jacsau.5c0005910.1021/jacsau.5c00059
Faycel Djebbar, Lise-Marie Chamoreau and Guillaume Lefèvre*,
{"title":"Influence of a Two-Fold Ligation Pattern on Iron-Mediated Aryl–Heteroaryl Cross-Electrophile Couplings","authors":"Faycel Djebbar, Lise-Marie Chamoreau and Guillaume Lefèvre*, ","doi":"10.1021/jacsau.5c0005910.1021/jacsau.5c00059","DOIUrl":"https://doi.org/10.1021/jacsau.5c00059https://doi.org/10.1021/jacsau.5c00059","url":null,"abstract":"<p >An aryl–heteroaryl cross-electrophile coupling (XEC) relying on the use of a single, well-defined iron catalyst is disclosed, involving magnesium as an electron source as well as heteroaryl chlorides and aryl iodides or bromides as coupling partners. A 2-fold coordination pattern featuring a π-acceptor, redox-active (N,N) ligand, along with a σ-donating phosphine ensures both the two-electron reduction of the starting iron(II) precursor to enter the cycle and access to stable organoiron(II) resting states, inhibiting the reductive decomposition of the catalyst.</p>","PeriodicalId":94060,"journal":{"name":"JACS Au","volume":"5 5","pages":"2135–2147 2135–2147"},"PeriodicalIF":8.5,"publicationDate":"2025-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/jacsau.5c00059","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144133933","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}