Zhao Li, Yi Li, Yang Zhan, Xiaodong Lin, Yingying Yao, Tianshuo Zhao, Fengzhan Sun, Hao Xu, Zhewen Ma, Wei Zhang, Yanling Xue, Xiaolong Li, Alexandru Vlad, Jianxin Zou
{"title":"On the Origin of Capacity Increase in Rechargeable Magnesium Batteries with Manganese Oxide Cathodes and Copper Metal Current Collectors","authors":"Zhao Li, Yi Li, Yang Zhan, Xiaodong Lin, Yingying Yao, Tianshuo Zhao, Fengzhan Sun, Hao Xu, Zhewen Ma, Wei Zhang, Yanling Xue, Xiaolong Li, Alexandru Vlad, Jianxin Zou","doi":"10.1002/anie.202416960","DOIUrl":"https://doi.org/10.1002/anie.202416960","url":null,"abstract":"Rechargeable magnesium batteries (RMBs), with Cu as positive electrode current collector (CC), typically display a gradual capacity increase with cycling. Whereas the origin of this was suggested in gradual active material electro‐activation, the fact that this is prevalent in many positive electrode material systems remains unexplained. Herein, we elucidate the underlying mechanism through a series of multiscale joint operando X‐ray characterizations, including operando synchrotron X‐ray diffraction and imaging technology. We select a series of manganese oxides as benchmark positive electrodes and find that no magnesium ions are stored within the lattices of these materials, despite an apparent cell capacity increase with cycling. The origin of capacity increase is rooted in the gradual electrochemical corrosion of metallic Cu, release of Cu(I, II) species in electrolyte, and their subsequent redox activity, resulting in apparent electrode capacity gains. Furthermore, the shuttle and redox speciation of Cu ions trigger the irreversible depletion of both the Cu CC (or any other source) and the magnesium metal, ultimately leading to cell failure. Our work suggests the need to reconsider the appropriateness of using Cu as a positive electrode CC for RMBs.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"176 1","pages":""},"PeriodicalIF":16.6,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142599596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jonathan Russell Nitschke, Amit Ghosh, John D Thoburn
{"title":"Light-Responsive Aldehyde-Reduction Catalysis Through Catalyst Encapsulation","authors":"Jonathan Russell Nitschke, Amit Ghosh, John D Thoburn","doi":"10.1002/anie.202419575","DOIUrl":"https://doi.org/10.1002/anie.202419575","url":null,"abstract":"We report a light-responsive tetrahedral metal–organic capsule that binds a perrhenate catalyst, which is released selectively upon irradiation with 350 nm light, turning on the catalytic reduction of organic carbonyls by hydrosilanes. The catalytic activity can be switched off by heating at 75 °C for 2.5 h, which stimulates capsule reformation and catalyst re-encapsulation. Multiple on-off cycles were shown, with a clear relationship between product yield and light irradiation time. Encapsulation thus enables the coupling of light-responsiveness to catalysis in a manner that might be generalized to other catalysts and capsules.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"17 1","pages":""},"PeriodicalIF":16.6,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142599976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Wanmin Chen, Na Xu, Lei Qin, Yi-Fei Deng, Gui-Lin Zhuang, Zhe Zhang, Ting-Zheng Xie, Pingshan Wang, Zhiping Zheng
{"title":"A Hollowed-Out Heterometallic Cluster for Catalytic Knoevenagel Condensation","authors":"Wanmin Chen, Na Xu, Lei Qin, Yi-Fei Deng, Gui-Lin Zhuang, Zhe Zhang, Ting-Zheng Xie, Pingshan Wang, Zhiping Zheng","doi":"10.1002/anie.202420770","DOIUrl":"https://doi.org/10.1002/anie.202420770","url":null,"abstract":"Lanthanide-containing clusters are synthetically Lanthanide-containing clusters are synthetically challenging and with significant chemical and materials applications. Herein, two isostructural heterometallic clusters of the formula (NO3)12@[Ln132Ni78(OH)292(IDA)48(CH3COO)96(NO3)12(H2O)78]Cl44·xH2O·yCH3OH (IDA = iminodiacetate; Ln = Gd 1, x = 110, y = 0; Ln = Eu 2, x = 95, y = 40) were obtained via co-hydrolysis of Ln3+ (Gd3+ or Eu3+) and Ni2+ in the presence of iminodiacetate (IDA). Crystallographic studies show that each features a truncated tetrahedral core of Ln132Ni78 within which a void of 5.5 Å in diameter; connecting the central cage and its exterior are four trumpet-like passageways surface-decorated with dinuclear units of [Gd(μ3-OH)2Gd]. Mass spectroscopic analyses indicate that both clusters maintained their structural integrity in aqueous solution, with cryo-electron microscopy providing the most convincing visual evidence in support of the cluster's solution stability. Size-selective Knoevenagel condensation, believed to occur in the passageways on the basis of experimental and molecular modeling results, was achieved in the presence of 1. The application of 1 as a uniquely structured molecular reactor and a recyclable heterogeneous catalyst was further illustrated by the one-pot three-component synthesis of biologically and pharmaceutically significant 4H-pyran derivatives.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"69 1","pages":""},"PeriodicalIF":16.6,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142600000","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Munise N. Karacan, Adelina Yafasova, Emil L. Fosbøl, Amine Tas, Katia Al-Chaer, Anna Gundlund, Finn Gustafsson, Anna Stahl, Morten Schou, Emil Wolsk, Nadia P. Dridi, Lars Køber, Jawad H. Butt
{"title":"Long-term risk of heart failure in patients with postoperative atrial fibrillation following non-cardiac surgery: Insights from a nationwide cohort","authors":"Munise N. Karacan, Adelina Yafasova, Emil L. Fosbøl, Amine Tas, Katia Al-Chaer, Anna Gundlund, Finn Gustafsson, Anna Stahl, Morten Schou, Emil Wolsk, Nadia P. Dridi, Lars Køber, Jawad H. Butt","doi":"10.1002/ejhf.3518","DOIUrl":"https://doi.org/10.1002/ejhf.3518","url":null,"abstract":"Atrial fibrillation (AF) is associated with heart failure (HF). However, it is unclear if postoperative AF (POAF) following non-cardiac surgery differs from non-surgical AF in terms of the risk of HF. We compared the long-term rate of incident HF in patients developing new-onset POAF following non-cardiac surgery with patients who did not develop POAF following non-cardiac surgery and patients with non-surgical non-valvular AF (NVAF).","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"6 1","pages":""},"PeriodicalIF":18.2,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142599910","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lindsey M Pale, Jude B Khatib, Alexandra Nusawardhana, Joshua Straka, Claudia M Nicolae, George-Lucian Moldovan
{"title":"CRISPR knockout genome-wide screens identify the HELQ-RAD52 axis in regulating the repair of cisplatin-induced single-stranded DNA gaps","authors":"Lindsey M Pale, Jude B Khatib, Alexandra Nusawardhana, Joshua Straka, Claudia M Nicolae, George-Lucian Moldovan","doi":"10.1093/nar/gkae998","DOIUrl":"https://doi.org/10.1093/nar/gkae998","url":null,"abstract":"Treatment with genotoxic agents, such as platinum compounds, is still the mainstay therapeutical approach for the majority of cancers. Our understanding of the mechanisms of action of these drugs is, however, imperfect and continuously evolving. Recent advances highlighted single-stranded DNA (ssDNA) gap accumulation as a potential determinant underlying cisplatin chemosensitivity, at least in some genetic backgrounds, such as BRCA mutations. Cisplatin-induced ssDNA gaps form upon restart of DNA synthesis downstream of cisplatin-induced lesions through repriming catalyzed by the PRIMPOL enzyme. Here, we show that PRIMPOL overexpression in otherwise wild-type cells results in accumulation of cisplatin-induced ssDNA gaps without sensitizing cells to cisplatin, suggesting that ssDNA gap accumulation does not confer cisplatin sensitivity in BRCA-proficient cells. To understand how ssDNA gaps may cause cellular sensitivity, we employed CRISPR-mediated genome-wide genetic screening to identify factors which enable the cytotoxicity of cisplatin-induced ssDNA gaps. We found that the helicase HELQ specifically suppresses cisplatin sensitivity in PRIMPOL-overexpressing cells, and this is associated with reduced ssDNA accumulation. We moreover identify RAD52 as a mediator of this pathway. RAD52 promotes ssDNA gap accumulation through a BRCA-mediated mechanism. Our work identified the HELQ-RAD52-BRCA axis as a regulator of ssDNA gap processing and cisplatin sensitization.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"8 1","pages":""},"PeriodicalIF":14.9,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142600992","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"PWOs repress gene transcription by regulating chromatin structures in Arabidopsis","authors":"Tingting Yang, Dingyue Wang, Lingxiao Luo, Xiaochang Yin, Zhihan Song, Minqi Yang, Yue Zhou","doi":"10.1093/nar/gkae958","DOIUrl":"https://doi.org/10.1093/nar/gkae958","url":null,"abstract":"PWWP-DOMAIN INTERACTOR OF POLYCOMBS (PWO) family proteins play a vital role in regulating plant development. However, the molecular mechanisms of how PWOs regulate chromatin structure is elusive. Our data show that the PWO1 binding sites are enriched with positive modifications but exclusive with H3K27me3. Moreover, PWO1 binds to the H3K27me3-enriched compartment domain (H3K27me3-CD) boundary regions, and functions to maintain the boundary strength. Meanwhile, we found that PWOs and Polycomb repressive complex 2 (PRC2) function parallelly in maintaining H3K27me3-CDs’ structure. Loss of either PWOs or PRC2 leads to H3K27me3-CD strength reduction, B to A compartment switching as well as the H3K27me3-CD relocating away from the nuclear periphery. Additionally, PWOs and lamin-like proteins collaborate to regulate multiple chromatin structures to repress gene transcription within H3K27me3-CDs. We conclude that PWOs maintain H3K27me3-CDs’ repressive state and regulate their spatial position in the nucleus.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"69 1","pages":""},"PeriodicalIF":14.9,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142599566","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Risa Ebihara, Takahiro Nakama, Ken Morishima, Maho Yagi-Utsumi, Masaaki Sugiyama, Daishi Fujita, Sota Sato, Makoto Fujita
{"title":"Physical Isolation of Single Protein Molecules within Well-Defined Coordination Cages to Enhance Their Stability","authors":"Risa Ebihara, Takahiro Nakama, Ken Morishima, Maho Yagi-Utsumi, Masaaki Sugiyama, Daishi Fujita, Sota Sato, Makoto Fujita","doi":"10.1002/anie.202419476","DOIUrl":"https://doi.org/10.1002/anie.202419476","url":null,"abstract":"Encapsulation of a single protein within a confined space can lead to distinct properties compared to bulk solutions, but controlling the number of encapsulated proteins and their environment remains challenging. This study demonstrates the encapsulation of single proteins within well-defined, tunable cavities of self-assembled coordination cages, thereby enhancing protein stability. Within uniform cavities of size-tunable coordination cages, 15 different proteins of varying sizes (3-6 nm in diameter) and properties (e.g., isoelectric points and hydrophobicity) were successfully confined. Various analytical techniques confirmed that the proteins maintained their secondary structures and enzymatic activities under denaturing conditions such as exposure to organic solvents, heat, and buffers. These findings suggest that such coordination cages have the potential to serve as synthetic hosts for precisely controlling protein functions within their customizable cavities.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"29 1","pages":""},"PeriodicalIF":16.6,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142600004","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Strong Replaces Weak: Hydrogen Bond-Anchored Electrolyte Enabling Ultra-Stable and Wide-Temperature Aqueous Zinc-Ion Capacitors","authors":"Zhongyou Peng, Ling Tang, Shulong Li, Licheng Tan, Yiwang Chen","doi":"10.1002/anie.202418242","DOIUrl":"https://doi.org/10.1002/anie.202418242","url":null,"abstract":"Despite aqueous electrolytes offer a great opportunity for large-scale energy storage owing to their safety and cost-effectiveness, their practical application suffers from the parasitic side reactions and poor temperature adaptability stemming from weak hydrogen-bond (HB) network in free water. Here, we propose the guiding thought “strong replaces weak” to design hydrogen bond-anchored electrolyte by introducing sulfolane (SL) for disrupting the regular weak HB network and contributing to superior temperature tolerance. Judiciously combined experimental characterization and theoretical calculation confirm that SL can remodel the primary solvation shell of metal ions, customize stable electrode interface chemistry and restrain the side reactions. Consequently, symmetric supercapacitor constructed by activated carbon (AC) electrodes is able to fully work within a voltage range of 2.4 V and reach high capacitance retention of 89.8% after 60000 cycles. Additionally, Zn anodes exhibit ultra-stable Zn plating/stripping behaviors and a wide temperature range (-20 ~ 60 °C), and zinc-ion capacitor (Zn//AC) also delivers an excellent cycling stability with capacity retention of 99.7% after 55000 cycles, implying that the designed electrolyte has practical application potential in extreme environments. This work proposes a novel critical solvation strategy that paves the route for the construction of ultra-stable and wide-temperature aqueous energy storage devices.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"216 1","pages":""},"PeriodicalIF":16.6,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142600006","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Gamal Ahmed Elfar, Obed Aning, Tsz Wai Ngai, Pearlyn Yeo, Joel Wai Kit Chan, Shang Hong Sim, Leonard Goh, Ju Yuan, Cheryl Zi Jin Phua, Joanna Zhen Zhen Yeo, Shi Ya Mak, Brian Kim Poh Goh, Pierce Kah-Hoe Chow, Wai Leong Tam, Ying Swan Ho, Chit Fang Cheok
{"title":"p53-dependent crosstalk between DNA replication integrity and redox metabolism mediated through a NRF2-PARP1 axis.","authors":"Gamal Ahmed Elfar, Obed Aning, Tsz Wai Ngai, Pearlyn Yeo, Joel Wai Kit Chan, Shang Hong Sim, Leonard Goh, Ju Yuan, Cheryl Zi Jin Phua, Joanna Zhen Zhen Yeo, Shi Ya Mak, Brian Kim Poh Goh, Pierce Kah-Hoe Chow, Wai Leong Tam, Ying Swan Ho, Chit Fang Cheok","doi":"10.1093/nar/gkae811","DOIUrl":"10.1093/nar/gkae811","url":null,"abstract":"<p><p>Mechanisms underlying p53-mediated protection of the replicating genome remain elusive, despite the quintessential role of p53 in maintaining genomic stability. Here, we uncover an unexpected function of p53 in curbing replication stress by limiting PARP1 activity and preventing the unscheduled degradation of deprotected stalled forks. We searched for p53-dependent factors and elucidated RRM2B as a prime factor. Deficiency in p53/RRM2B results in the activation of an NRF2 antioxidant transcriptional program, with a concomitant elevation in basal PARylation in cells. Dissecting the consequences of p53/RRM2B loss revealed a crosstalk between redox metabolism and genome integrity that is negotiated through a hitherto undescribed NRF2-PARP1 axis, and pinpoint G6PD as a primary oxidative stress-induced NRF2 target and activator of basal PARylation. This study elucidates how loss of p53 could be destabilizing for the replicating genome and, importantly, describes an unanticipated crosstalk between redox metabolism, PARP1 and p53 tumor suppressor pathway that is broadly relevant in cancers and can be leveraged therapeutically.</p>","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":" ","pages":"12351-12377"},"PeriodicalIF":16.6,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11551750/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142308250","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Vincent Lombard, Bernard Henrissat, Marie-Line Garron
{"title":"CAZac: an activity descriptor for carbohydrate-active enzymes","authors":"Vincent Lombard, Bernard Henrissat, Marie-Line Garron","doi":"10.1093/nar/gkae1045","DOIUrl":"https://doi.org/10.1093/nar/gkae1045","url":null,"abstract":"The Carbohydrate-Active enZYme database (CAZy; www.cazy.org) has been providing the reference classification of carbohydrate-active enzymes (CAZymes) for &gt;30 years. Based on literature survey, the sequence-based families of CAZymes are enriched with functional data by using the International Union of Biochemistry and Molecular Biology Enzyme Commission (EC) number system. However, this system was not developed to search or compare functional information. To better harness functional information, we have developed CAZac (CAZyme activity descriptor), a multicriterion system that describes CAZymes’ mechanisms, glycosidic bond orientations, subsites and inter-residue connectivities. This new system, implemented for glycoside hydrolases, glycoside phosphorylases, transglycosidases, polysaccharide lyases and lytic polysaccharide monooxygenases allows complex searches in the CAZy database to uncover the evolution of substrate specificity and mechanisms of CAZymes across families.","PeriodicalId":16,"journal":{"name":"ACS Energy Letters ","volume":"24 1","pages":""},"PeriodicalIF":14.9,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142598301","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}