S. Wang, Tai Wu, Jingjing Guo, Rongjun Zhao, Yong Hua, Yanli Zhao
{"title":"Engineering the Hole Transport Layer with a Conductive Donor–Acceptor Covalent Organic Framework for Stable and Efficient Perovskite Solar Cells","authors":"S. Wang, Tai Wu, Jingjing Guo, Rongjun Zhao, Yong Hua, Yanli Zhao","doi":"10.1021/acscentsci.4c00416","DOIUrl":"https://doi.org/10.1021/acscentsci.4c00416","url":null,"abstract":"","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141344389","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"ACS Central Science Virtual Issue on Advanced Materials and Processes for Building Low-Carbon Energy Systems","authors":"Chengyi Hu, Nanfeng Zheng","doi":"10.1021/acscentsci.4c00925","DOIUrl":"https://doi.org/10.1021/acscentsci.4c00925","url":null,"abstract":"","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141342323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Raj V. Nithun, Yumi Minyi Yao, O. Harel, Shaimaa Habiballah, Ariel Afek, Muhammad Jbara
{"title":"Site-Specific Acetylation of the Transcription Factor Protein Max Modulates Its DNA Binding Activity","authors":"Raj V. Nithun, Yumi Minyi Yao, O. Harel, Shaimaa Habiballah, Ariel Afek, Muhammad Jbara","doi":"10.1021/acscentsci.4c00686","DOIUrl":"https://doi.org/10.1021/acscentsci.4c00686","url":null,"abstract":"","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141353124","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
F. Aaron Cruz-Navarrete, Wezley C. Griffin, Yuk-Cheung Chan, Maxwell I. Martin, Jose L. Alejo, Ryan A. Brady, S. Kundhavai Natchiar, Isaac J. Knudson, Roger B. Altman, Alanna Schepartz, Scott J. Miller, Scott C. Blanchard
{"title":"β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism","authors":"F. Aaron Cruz-Navarrete, Wezley C. Griffin, Yuk-Cheung Chan, Maxwell I. Martin, Jose L. Alejo, Ryan A. Brady, S. Kundhavai Natchiar, Isaac J. Knudson, Roger B. Altman, Alanna Schepartz, Scott J. Miller, Scott C. Blanchard","doi":"10.1021/acscentsci.4c00314","DOIUrl":"https://doi.org/10.1021/acscentsci.4c00314","url":null,"abstract":"Templated synthesis of proteins containing non-natural amino acids (nnAAs) promises to expand the chemical space available to biological therapeutics and materials, but existing technologies are still limiting. Addressing these limitations requires a deeper understanding of the mechanism of protein synthesis and how it is perturbed by nnAAs. Here we examine the impact of nnAAs on the formation and ribosome utilization of the central elongation substrate: the ternary complex of native, aminoacylated tRNA, thermally unstable elongation factor, and GTP. By performing ensemble and single-molecule fluorescence resonance energy transfer measurements, we reveal that both the (<i>R</i>)- and (<i>S</i>)-β<sup>2</sup> isomers of phenylalanine (Phe) disrupt ternary complex formation to levels below in vitro detection limits, while (<i>R</i>)- and (<i>S</i>)-β<sup>3</sup>-Phe reduce ternary complex stability by 1 order of magnitude. Consistent with these findings, (<i>R</i>)- and (<i>S</i>)-β<sup>2</sup>-Phe-charged tRNAs were not utilized by the ribosome, while (<i>R</i>)- and (<i>S</i>)-β<sup>3</sup>-Phe stereoisomers were utilized inefficiently. (<i>R</i>)-β<sup>3</sup>-Phe but not (<i>S</i>)-β<sup>3</sup>-Phe also exhibited order of magnitude defects in the rate of translocation after mRNA decoding. We conclude from these findings that non-natural amino acids can negatively impact the translation mechanism on multiple fronts and that the bottlenecks for improvement must include the consideration of the efficiency and stability of ternary complex formation.","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141258753","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"PEARL-Catalyzed Peptide Bond Formation after Chain Reversal by Ureido-Forming Condensation Domains","authors":"Yue Yu, Wilfred A. van der Donk","doi":"10.1021/acscentsci.4c00044","DOIUrl":"https://doi.org/10.1021/acscentsci.4c00044","url":null,"abstract":"A subset of nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs) are encoded in their biosynthetic gene clusters (BGCs) with enzymes annotated as lantibiotic dehydratases. The functions of these putative lantibiotic dehydratases remain unknown. Here, we characterize an NRPS-PKS BGC with a putative lantibiotic dehydratase from the bacterium <i>Stackebrandtia nassauensis</i> (<i>sna</i>). Heterologous expression revealed several metabolites produced by the BGC, and the omission of selected biosynthetic enzymes revealed the biosynthetic pathway toward these compounds. The final product is a bisarginyl ureidopeptide with an enone electrophile. The putative lantibiotic dehydratase catalyzes peptide bond formation to a Thr that extends the peptide scaffold opposite to the NRPS and PKS biosynthetic direction. The condensation domain of the NRPS SnaA catalyzes the formation of a ureido group, and bioinformatics analysis revealed a distinct active site signature EHHXXHDG of ureido-generating condensation (C<sub>urea</sub>) domains. This work demonstrates that the annotated lantibiotic dehydratase serves as a separate amide bond-forming machinery in addition to the NRPS, and that the lantibiotic dehydratase enzyme family possesses diverse catalytic activities in the biosynthesis of both ribosomal and nonribosomal natural products.","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141258499","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Mitochondrial Thermogenesis Can Trigger Heat Shock Response in the Nucleus","authors":"Myeong-Gyun Kang, Hwa-Ryeon Kim, Hee Yong Lee, Chulhwan Kwak, Hyewon Koh, Byoung Heon Kang, Jae-Seok Roe, Hyun-Woo Rhee","doi":"10.1021/acscentsci.3c01589","DOIUrl":"https://doi.org/10.1021/acscentsci.3c01589","url":null,"abstract":"Mitochondrial thermogenesis is a process in which heat is generated by mitochondrial respiration. In living organisms, the thermogenic mechanisms that maintain body temperature have been studied extensively in fat cells with little knowledge on how mitochondrial heat may act beyond energy expenditure. Here, we highlight that the exothermic oxygen reduction reaction (Δ<i>H</i><sub>f</sub>° = −286 kJ/mol) is the main source of the protonophore-induced mitochondrial thermogenesis, and this heat is conducted to other cellular organelles, including the nucleus. As a result, mitochondrial heat that reached the nucleus initiated the classical heat shock response, including the formation of nuclear stress granules and the localization of heat shock factor 1 (HSF1) to chromatin. Consequently, activated HSF1 increases the level of gene expression associated with the response to thermal stress in mammalian cells. Our results illustrate heat generated within the cells as a potential source of mitochondria-nucleus communication and expand our understanding of the biological functions of mitochondria in cell physiology.","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141258496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Kaitlin L. Branch, Erin R. Johnson, Eva M. Nichols
{"title":"Porphyrin Aggregation under Homogeneous Conditions Inhibits Electrocatalysis: A Case Study on CO2 Reduction","authors":"Kaitlin L. Branch, Erin R. Johnson, Eva M. Nichols","doi":"10.1021/acscentsci.4c00121","DOIUrl":"https://doi.org/10.1021/acscentsci.4c00121","url":null,"abstract":"Metalloporphyrins are widely used as homogeneous electrocatalysts for transformations relevant to clean energy and sustainable organic synthesis. Metalloporphyrins are well-known to aggregate due to π–π stacking, but surprisingly, the influence of aggregation on homogeneous electrocatalytic performance has not been investigated previously. Herein, we present three structurally related iron <i>meso</i>-phenylporphyrins whose aggregation properties are different in commonly used <i>N</i>,<i>N</i>-dimethylformamide (DMF) electrolyte. Both spectroscopy and light scattering provide evidence of extensive porphyrin aggregation under conventional electrocatalytic conditions. Using the electrocatalytic reduction of CO<sub>2</sub> to CO as a test reaction, cyclic voltammetry reveals an inverse dependence of the kinetics on the catalyst concentration. The inhibition extends to bulk performance, where up to 75% of the catalyst at 1 mM is inactive compared to at 0.25 mM. We additionally report how aggregation is perturbed by organic additives, axial ligands, and redox state. Periodic boundary calculations provide additional insights into aggregate stability as a function of metalloporphyrin structure. Finally, we generalize the aggregation phenomenon by surveying metalloporphyrins with different metals and substituents. This study demonstrates that homogeneous metalloporphyrins can aggregate severely in well-solubilizing organic electrolytes, that aggregation can be easily modulated through experimental conditions, and that the extent of aggregation must be considered for accurate catalytic benchmarking.","PeriodicalId":10,"journal":{"name":"ACS Central Science","volume":null,"pages":null},"PeriodicalIF":18.2,"publicationDate":"2024-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141258262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}