Pub Date : 2025-10-23DOI: 10.1038/s41929-025-01427-1
Zhihao Cui, Kassidy D. Aztergo, Jiseon Hwang, Anne C. Co
CO adsorption free energy ( $$Delta {G}_{{rm{C}}{rm{O}}}^{{rm{a}}{rm{d}}{rm{s}}}$$ ) has been proposed as a key descriptor for CO2 electroreduction (CO2R), yet its role remains unverified due to the lack of experimental methods capable of probing $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ under reaction conditions. Here we present a kinetic model combined with a rotating ring-disk electrode voltammetry method to estimate $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ on the active sites of various CO-producing catalysts during CO2R. Our results reveal that CO adsorption is influenced by multiple factors including catalyst type, cation identity and concentration, applied potential and surface structure. Notably, the measured difference in $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ between Au and Cu at CO2R-to-CO active sites is small, suggesting that the $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ of CO-producing active sites alone cannot account for Cu’s unique ability to catalyse CO2 into multicarbon products at appreciable rates. This study highlights the complexity of evaluating CO adsorption under CO2R conditions and introduces a robust experimental framework for quantifying $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ on CO-producing catalysts. CO adsorption free energy has been suggested as a descriptor to explain and predict CO2 reduction activity across various electrocatalysts, but methods for determining it experimentally under operating conditions are lacking. Here a kinetic model is combined with rotating ring-disk voltammetry to estimate this parameter.
{"title":"Determining CO adsorption free energies on CO2 electroreduction active sites through kinetic analysis","authors":"Zhihao Cui, Kassidy D. Aztergo, Jiseon Hwang, Anne C. Co","doi":"10.1038/s41929-025-01427-1","DOIUrl":"10.1038/s41929-025-01427-1","url":null,"abstract":"CO adsorption free energy ( $$Delta {G}_{{rm{C}}{rm{O}}}^{{rm{a}}{rm{d}}{rm{s}}}$$ ) has been proposed as a key descriptor for CO2 electroreduction (CO2R), yet its role remains unverified due to the lack of experimental methods capable of probing $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ under reaction conditions. Here we present a kinetic model combined with a rotating ring-disk electrode voltammetry method to estimate $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ on the active sites of various CO-producing catalysts during CO2R. Our results reveal that CO adsorption is influenced by multiple factors including catalyst type, cation identity and concentration, applied potential and surface structure. Notably, the measured difference in $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ between Au and Cu at CO2R-to-CO active sites is small, suggesting that the $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ of CO-producing active sites alone cannot account for Cu’s unique ability to catalyse CO2 into multicarbon products at appreciable rates. This study highlights the complexity of evaluating CO adsorption under CO2R conditions and introduces a robust experimental framework for quantifying $$Delta {G}_{mathrm{CO}}^{mathrm{ads}}$$ on CO-producing catalysts. CO adsorption free energy has been suggested as a descriptor to explain and predict CO2 reduction activity across various electrocatalysts, but methods for determining it experimentally under operating conditions are lacking. Here a kinetic model is combined with rotating ring-disk voltammetry to estimate this parameter.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1117-1127"},"PeriodicalIF":44.6,"publicationDate":"2025-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371981","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}
Pub Date : 2025-10-23DOI: 10.1038/s41929-025-01421-7
Paula Sebastián-Pascual, Antonia Herzog, Yirui Zhang, Yang Shao-Horn, María Escudero-Escribano
Electrolyte effects play a fundamental role in electrocatalysis, influencing reaction kinetics, selectivity and catalyst stability by altering interfacial interactions and charge distribution. Here we report recent advances to rationalize non-covalent interactions between electrolyte and surface adsorbates in electrocatalysis. Three main schools of thought have rationalized the effect of electrolyte–adsorbates–surface interactions on the reaction kinetics, each based on different descriptors. The first suggests that non-covalent interactions with the electrolyte modify the binding energies of the adsorbed intermediates. The second highlights the role of charge and electric fields near the electric double layer, shaped by the potential of zero charge, in stabilizing the polar adsorbates and governing proton transfer. The third focuses on energy barriers arising from the restructuring of the water solvation spheres of both electrolyte and reactants. We critically examine the main arguments and limitations of each framework, with a focus on hydrogen evolution and carbon dioxide reduction, and outline experimental challenges and future directions for elucidating electrolyte effects in electrocatalysis. The structure and properties of the electric double layer that forms at the electrode–electrolyte interface is crucial in determining the performance of electrocatalytic reactions. This Perspective puts forward and discusses three major schools of thought on electrolyte effects and electrocatalyst design.
{"title":"Electrolyte effects in proton–electron transfer reactions and implications for renewable fuels and chemicals synthesis","authors":"Paula Sebastián-Pascual, Antonia Herzog, Yirui Zhang, Yang Shao-Horn, María Escudero-Escribano","doi":"10.1038/s41929-025-01421-7","DOIUrl":"10.1038/s41929-025-01421-7","url":null,"abstract":"Electrolyte effects play a fundamental role in electrocatalysis, influencing reaction kinetics, selectivity and catalyst stability by altering interfacial interactions and charge distribution. Here we report recent advances to rationalize non-covalent interactions between electrolyte and surface adsorbates in electrocatalysis. Three main schools of thought have rationalized the effect of electrolyte–adsorbates–surface interactions on the reaction kinetics, each based on different descriptors. The first suggests that non-covalent interactions with the electrolyte modify the binding energies of the adsorbed intermediates. The second highlights the role of charge and electric fields near the electric double layer, shaped by the potential of zero charge, in stabilizing the polar adsorbates and governing proton transfer. The third focuses on energy barriers arising from the restructuring of the water solvation spheres of both electrolyte and reactants. We critically examine the main arguments and limitations of each framework, with a focus on hydrogen evolution and carbon dioxide reduction, and outline experimental challenges and future directions for elucidating electrolyte effects in electrocatalysis. The structure and properties of the electric double layer that forms at the electrode–electrolyte interface is crucial in determining the performance of electrocatalytic reactions. This Perspective puts forward and discusses three major schools of thought on electrolyte effects and electrocatalyst design.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"986-999"},"PeriodicalIF":44.6,"publicationDate":"2025-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371982","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}
Pub Date : 2025-10-23DOI: 10.1038/s41929-025-01425-3
Srividya Murali, Guo-Bin Hu, Dale F. Kreitler, Ana Arroyo Carriedo, Luke C. Lewis, Samuel Adu Fosu, Olivia G. Weaver, Ella M. Buzas, Kathryn M. Byerly, Yasuo Yoshikuni, Sean McSweeney, Hannah S. Shafaat, Justin A. North
Bacteria utilize methylthio-alkane reductase (MAR) to acquire sulfur from volatile organic sulfur compounds. Reductive cleavage of methylthio-ethanol and dimethylsulfide liberates methanethiol for methionine synthesis and concomitantly releases ethylene and methane, respectively. Here we show that the native MAR of Rhodospirillum rubrum is a two-component system composed of a MarH ATP-dependent reductase and a MarDK catalytic core, whose architecture parallels nitrogenase. MarS complexes with MarDK to downregulate MAR activity during cellular sulfate influx, based on chromatographic and activity analyses. MarDK possesses complex metallocofactors resembling, but not identical to, nitrogenase P- and iron-only M-clusters, designated as mar1 and mar2 clusters based on metal, spectroscopic and mutagenesis analyses. They exhibit electronic features similar to the iron-only nitrogenase under turnover and, remarkably, are matured by MarB or nitrogenase NifB, resulting in maturase-dependent activity profiles. Altogether, this suggests a broader scope of reactivity, mechanisms and regulation in microbial metabolism for the nitrogenase-like family of enzymes than previously considered. Insights into the mechanism of methylthio-alkane reductase (MAR)—a nitrogenase-like enzyme essential for growth under sulfate-limited conditions—have remained scarce. Now a cryo-EM structure of MAR from Rhodospirillum rubrum, along with spectroscopic investigations, reveals how it uses complex metallocofactors for catalysis.
细菌利用甲基硫烷还原酶（MAR）从挥发性有机硫化合物中获取硫。甲基硫乙醇和二甲基硫化物的还原裂解释放甲硫醇用于蛋氨酸合成，同时分别释放乙烯和甲烷。本研究表明红红螺旋藻的天然MAR是一个由MAR atp依赖性还原酶和markk催化核心组成的双组分体系，其结构与氮酶相似。基于色谱和活性分析，MarS复合物与markk在细胞硫酸盐流入过程中下调MAR活性。markk具有复杂的金属辅助因子，类似于氮化酶P-和铁- m -簇，但不完全相同，根据金属，光谱和诱变分析，被称为mar1和mar2簇。它们表现出与纯铁氮酶相似的电子特征，值得注意的是，它们被MarB或氮酶NifB成熟，从而产生依赖于成熟酶的活性谱。总之，这表明在微生物代谢中，类氮酶家族的反应性、机制和调控范围比以前认为的要广泛。甲基硫代烷烃还原酶（MAR）是一种在硫酸盐限制条件下生长所必需的类似于氮酶的酶，对其机制的了解仍然很少。现在，红红螺旋藻MAR的低温电镜结构，以及光谱研究，揭示了它是如何使用复杂的金属辅助因子进行催化的。
{"title":"Architecture, catalysis and regulation of methylthio-alkane reductase for bacterial sulfur acquisition from volatile organic compounds","authors":"Srividya Murali, Guo-Bin Hu, Dale F. Kreitler, Ana Arroyo Carriedo, Luke C. Lewis, Samuel Adu Fosu, Olivia G. Weaver, Ella M. Buzas, Kathryn M. Byerly, Yasuo Yoshikuni, Sean McSweeney, Hannah S. Shafaat, Justin A. North","doi":"10.1038/s41929-025-01425-3","DOIUrl":"10.1038/s41929-025-01425-3","url":null,"abstract":"Bacteria utilize methylthio-alkane reductase (MAR) to acquire sulfur from volatile organic sulfur compounds. Reductive cleavage of methylthio-ethanol and dimethylsulfide liberates methanethiol for methionine synthesis and concomitantly releases ethylene and methane, respectively. Here we show that the native MAR of Rhodospirillum rubrum is a two-component system composed of a MarH ATP-dependent reductase and a MarDK catalytic core, whose architecture parallels nitrogenase. MarS complexes with MarDK to downregulate MAR activity during cellular sulfate influx, based on chromatographic and activity analyses. MarDK possesses complex metallocofactors resembling, but not identical to, nitrogenase P- and iron-only M-clusters, designated as mar1 and mar2 clusters based on metal, spectroscopic and mutagenesis analyses. They exhibit electronic features similar to the iron-only nitrogenase under turnover and, remarkably, are matured by MarB or nitrogenase NifB, resulting in maturase-dependent activity profiles. Altogether, this suggests a broader scope of reactivity, mechanisms and regulation in microbial metabolism for the nitrogenase-like family of enzymes than previously considered. Insights into the mechanism of methylthio-alkane reductase (MAR)—a nitrogenase-like enzyme essential for growth under sulfate-limited conditions—have remained scarce. Now a cryo-EM structure of MAR from Rhodospirillum rubrum, along with spectroscopic investigations, reveals how it uses complex metallocofactors for catalysis.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1072-1085"},"PeriodicalIF":44.6,"publicationDate":"2025-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41929-025-01425-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371977","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-23DOI: 10.1038/s41929-025-01426-2
Ana Lago-Maciel, Jéssica C. Soares, Jan Zarzycki, Charles J. Buchanan, Tristan Reif-Trauttmansdorff, Frederik V. Schmidt, Stefano Lometto, Nicole Paczia, Jan M. Schuller, D. Flemming Hansen, Gabriella T. Heller, Simone Prinz, Georg K. A. Hochberg, Antonio J. Pierik, Johannes G. Rebelein
Methylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are classified as nitrogenase-like enzymes, despite lacking the ability to convert dinitrogen to ammonia, raising fundamental questions about the factors controlling their activity and specificity. Here we present the molecular structure of the methylthio-alkane reductase, which reveals large metalloclusters, including the P-cluster and the [Fe8S9C]-cluster, previously found only in nitrogenases. Our findings suggest that distinct metallocluster coordination, surroundings and substrate channels determine the activity of these related metalloenzymes. This study provides new insights into nitrogen fixation, sulfur-compound reduction and hydrocarbon production. We also shed light on the evolutionary history of P-cluster and [Fe8S9C]-cluster-containing reductases emerging before nitrogenases. Methylthio-alkane reductases are recently discovered enzymes that can produce methanethiol and small hydrocarbons from methylated sulfur compounds. Now the cryo-EM structure of a methylthio-alkane reductase complex is solved, revealing large metalloclusters previously observed only within nitrogenases.
{"title":"Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage","authors":"Ana Lago-Maciel, Jéssica C. Soares, Jan Zarzycki, Charles J. Buchanan, Tristan Reif-Trauttmansdorff, Frederik V. Schmidt, Stefano Lometto, Nicole Paczia, Jan M. Schuller, D. Flemming Hansen, Gabriella T. Heller, Simone Prinz, Georg K. A. Hochberg, Antonio J. Pierik, Johannes G. Rebelein","doi":"10.1038/s41929-025-01426-2","DOIUrl":"10.1038/s41929-025-01426-2","url":null,"abstract":"Methylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are classified as nitrogenase-like enzymes, despite lacking the ability to convert dinitrogen to ammonia, raising fundamental questions about the factors controlling their activity and specificity. Here we present the molecular structure of the methylthio-alkane reductase, which reveals large metalloclusters, including the P-cluster and the [Fe8S9C]-cluster, previously found only in nitrogenases. Our findings suggest that distinct metallocluster coordination, surroundings and substrate channels determine the activity of these related metalloenzymes. This study provides new insights into nitrogen fixation, sulfur-compound reduction and hydrocarbon production. We also shed light on the evolutionary history of P-cluster and [Fe8S9C]-cluster-containing reductases emerging before nitrogenases. Methylthio-alkane reductases are recently discovered enzymes that can produce methanethiol and small hydrocarbons from methylated sulfur compounds. Now the cryo-EM structure of a methylthio-alkane reductase complex is solved, revealing large metalloclusters previously observed only within nitrogenases.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1086-1099"},"PeriodicalIF":44.6,"publicationDate":"2025-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41929-025-01426-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371979","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-10DOI: 10.1038/s41929-025-01406-6
Sarah Laura Krausz, Dorottya Anna Simon, Zsuzsa Bartos, Zsuzsanna Biczók, Éva Varga, Krisztina Huszár, Péter István Kulcsár, András Tálas, Zoltán Ligeti, Ervin Welker
Prime editing (PE) is a promising gene editing method that exploits a reverse transcriptase fused to a Cas9, whose single guide RNA (sgRNA) is extended with a reverse transcriptase template containing the desired DNA modifications. Its efficiency and specificity are inconsistent, requiring extensive optimization. To address this, we propose prime editing with prolonged editing window (proPE), which uses a second non-cleaving sgRNA to target the reverse transcriptase template near the edit site. ProPE requires less optimization than PE and extends PE’s potential for allele-specific modifications. By overcoming five limitations of PE, proPE significantly increases overall editing efficiency 6.2-fold up to 29.3% for low-performing edits (<5% with PE) and broadens its applicability to modifications beyond the typical PE range, encompassing a major portion of human pathogenic single nucleotide polymorphisms. With these enhanced properties, proPE holds considerable promise for improved gene editing, including disease modelling and therapeutic intervention. Prime editing is a CRISPR methodology whose efficiency declines with distance from the target sequence. Here the authors demonstrate prime editing with prolonged editing window, proPE, which extends the editing distance, enabling the use of prime editing for therapeutic interventions.
{"title":"ProPE expands the prime editing window and enhances gene editing efficiency where prime editing is inefficient","authors":"Sarah Laura Krausz, Dorottya Anna Simon, Zsuzsa Bartos, Zsuzsanna Biczók, Éva Varga, Krisztina Huszár, Péter István Kulcsár, András Tálas, Zoltán Ligeti, Ervin Welker","doi":"10.1038/s41929-025-01406-6","DOIUrl":"10.1038/s41929-025-01406-6","url":null,"abstract":"Prime editing (PE) is a promising gene editing method that exploits a reverse transcriptase fused to a Cas9, whose single guide RNA (sgRNA) is extended with a reverse transcriptase template containing the desired DNA modifications. Its efficiency and specificity are inconsistent, requiring extensive optimization. To address this, we propose prime editing with prolonged editing window (proPE), which uses a second non-cleaving sgRNA to target the reverse transcriptase template near the edit site. ProPE requires less optimization than PE and extends PE’s potential for allele-specific modifications. By overcoming five limitations of PE, proPE significantly increases overall editing efficiency 6.2-fold up to 29.3% for low-performing edits (<5% with PE) and broadens its applicability to modifications beyond the typical PE range, encompassing a major portion of human pathogenic single nucleotide polymorphisms. With these enhanced properties, proPE holds considerable promise for improved gene editing, including disease modelling and therapeutic intervention. Prime editing is a CRISPR methodology whose efficiency declines with distance from the target sequence. Here the authors demonstrate prime editing with prolonged editing window, proPE, which extends the editing distance, enabling the use of prime editing for therapeutic interventions.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1100-1116"},"PeriodicalIF":44.6,"publicationDate":"2025-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41929-025-01406-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371985","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-06DOI: 10.1038/s41929-025-01418-2
Pan Xu, Duo-Sheng Wang, Zhenyu Zhu, X. Peter Zhang
Delocalized radical systems present a challenging yet appealing ground to test the control of multiple selectivity in organic synthesis. Despite some recent advances, the issue of regioselectivity in delocalized radical systems has largely centred on allylic radicals. To explore larger delocalized radical systems, we report the catalytic generation of extensively delocalized 4-vinylphenoxyl radicals and their involvement as key intermediates in regioselective radical C–N bond formation. Guided by the mechanistic principles of metalloradical catalysis, we develop a Co(II)-based enantioselective radical system for dearomative 1,7-conjugate amination of readily available 4-vinylphenols with aryl azides. This can afford valuable chiral α-tertiary amino acid derivatives in high yields with excellent enantioselectivities for the newly created tetrasubstituted stereocentres. Unlike previous systems, this amination involves hydrogen-atom abstraction from O–H bonds. As demonstrated with 1,6-conjugate addition with various nucleophiles, the resulting α-tertiary amino acid derivatives, which bear additional para-quinone methide functionality, may find useful synthetic applications. Delocalized radical systems are appealing for controlling stereoselectivity in organic synthesis. Here the authors report on a Co(II)-based enantioselective radical system for the dearomative 1,7-conjugate amination of readily available 4-vinylphenols with aryl azides.
{"title":"Enantioselective radical dearomative conjugate amination enabled by Co(II)-based metalloradical catalysis","authors":"Pan Xu, Duo-Sheng Wang, Zhenyu Zhu, X. Peter Zhang","doi":"10.1038/s41929-025-01418-2","DOIUrl":"10.1038/s41929-025-01418-2","url":null,"abstract":"Delocalized radical systems present a challenging yet appealing ground to test the control of multiple selectivity in organic synthesis. Despite some recent advances, the issue of regioselectivity in delocalized radical systems has largely centred on allylic radicals. To explore larger delocalized radical systems, we report the catalytic generation of extensively delocalized 4-vinylphenoxyl radicals and their involvement as key intermediates in regioselective radical C–N bond formation. Guided by the mechanistic principles of metalloradical catalysis, we develop a Co(II)-based enantioselective radical system for dearomative 1,7-conjugate amination of readily available 4-vinylphenols with aryl azides. This can afford valuable chiral α-tertiary amino acid derivatives in high yields with excellent enantioselectivities for the newly created tetrasubstituted stereocentres. Unlike previous systems, this amination involves hydrogen-atom abstraction from O–H bonds. As demonstrated with 1,6-conjugate addition with various nucleophiles, the resulting α-tertiary amino acid derivatives, which bear additional para-quinone methide functionality, may find useful synthetic applications. Delocalized radical systems are appealing for controlling stereoselectivity in organic synthesis. Here the authors report on a Co(II)-based enantioselective radical system for the dearomative 1,7-conjugate amination of readily available 4-vinylphenols with aryl azides.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1051-1061"},"PeriodicalIF":44.6,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145329335","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}
Renewable electricity-driven capture and conversion of oceanic dissolved inorganic carbon into value-added chemicals offers a sustainable route towards negative carbon emissions and a circular carbon economy. Here we present an artificial ocean carbon recycling system that captures and converts oceanic carbon sources into biochemicals through a decoupled electro-biocatalytic hybrid process. The system captures CO2 from natural seawater under very dilute yet realistic dissolved inorganic carbon conditions (2.16 mM) with high capture efficiency (>70%), low energy consumption (3 kWh kgCO2−1) and long stability (536 h). Techno-economic analysis revealed a competitive cost of capture (US$229.9 tCO2−1). Using a highly efficient and stable bismuth-based electrocatalyst, CO2 was further converted into pure formic acid (800 mA cm−2 at −1.37 V) and subsequently transformed by engineered Vibrio natriegens into succinic acid (1.37 g l−1). Therefore, our electro-bioconversion system represents a solution to sustainable biochemical synthesis using the ocean carbon sink as a resource. Tandem electro-biocatalytic systems present a versatile platform for producing a variety of synthetic products using CO2 as a starting material. Here direct ocean carbon capture is incorporated into an electrolysis scheme to produce formic acid from CO2 dissolved in seawater that is subsequently converted to succinate in a bioreactor.
可再生电力驱动的海洋溶解无机碳的捕获和转化为增值化学品，为实现负碳排放和循环碳经济提供了一条可持续的途径。在这里，我们提出了一个人工海洋碳回收系统，该系统通过解耦的电-生物催化混合过程捕获海洋碳源并将其转化为生物化学物质。该系统在非常稀释的自然海水中捕获二氧化碳，但实际的溶解无机碳条件（2.16 mM）具有高捕获效率（>70%），低能耗（3 kWh kgCO2−1）和长稳定性（536小时）。技术经济分析显示，捕集具有竞争力的成本（229.9吨二氧化碳−1美元）。利用高效稳定的铋基电催化剂，将CO2进一步转化为纯甲酸（800 mA cm - 2，电压为- 1.37 V），然后通过工程弧菌将其转化为琥珀酸（1.37 g l - 1）。因此，我们的电-生物转换系统代表了利用海洋碳汇作为资源的可持续生化合成的解决方案。串联电-生物催化系统提供了一个通用的平台，用于生产各种合成产品，使用二氧化碳作为起始材料。在这里，直接的海洋碳捕获被纳入电解方案，从溶解在海水中的二氧化碳中产生甲酸，随后在生物反应器中转化为琥珀酸盐。
{"title":"Efficient and scalable upcycling of oceanic carbon sources into bioplastic monomers","authors":"Chengbo Li, Mingming Guo, Bo Yang, Yuan Ji, Jing Zhang, Liujiang Zhou, Chunxiao Liu, Haoyuan Wang, Jiawei Li, Weiqing Xue, Xinyan Zhang, Hongliang Zeng, Yanjiang Wang, Donghao Zhao, Kexin Zhong, Shanshan Pi, Minzhe Hei, Xu Li, Qiu Jiang, Tingting Zheng, Xiang Gao, Chuan Xia","doi":"10.1038/s41929-025-01416-4","DOIUrl":"10.1038/s41929-025-01416-4","url":null,"abstract":"Renewable electricity-driven capture and conversion of oceanic dissolved inorganic carbon into value-added chemicals offers a sustainable route towards negative carbon emissions and a circular carbon economy. Here we present an artificial ocean carbon recycling system that captures and converts oceanic carbon sources into biochemicals through a decoupled electro-biocatalytic hybrid process. The system captures CO2 from natural seawater under very dilute yet realistic dissolved inorganic carbon conditions (2.16 mM) with high capture efficiency (>70%), low energy consumption (3 kWh kgCO2−1) and long stability (536 h). Techno-economic analysis revealed a competitive cost of capture (US$229.9 tCO2−1). Using a highly efficient and stable bismuth-based electrocatalyst, CO2 was further converted into pure formic acid (800 mA cm−2 at −1.37 V) and subsequently transformed by engineered Vibrio natriegens into succinic acid (1.37 g l−1). Therefore, our electro-bioconversion system represents a solution to sustainable biochemical synthesis using the ocean carbon sink as a resource. Tandem electro-biocatalytic systems present a versatile platform for producing a variety of synthetic products using CO2 as a starting material. Here direct ocean carbon capture is incorporated into an electrolysis scheme to produce formic acid from CO2 dissolved in seawater that is subsequently converted to succinate in a bioreactor.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1023-1037"},"PeriodicalIF":44.6,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371984","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}
Pub Date : 2025-09-29DOI: 10.1038/s41929-025-01417-3
Chenggong Jiang, Bill Yan, Bryan R. Goldsmith, Suljo Linic
The metal–support interaction (MSI) critically influences the performance of supported nanocatalysts and their long-term stability, yet the factors governing MSIs are multifaceted and challenging to sort out. Here we combine first-principles neural network molecular dynamics (NN-MD) simulations with interpretable machine learning (iML) to shed light on the factors determining MSIs for Pt nanoparticles on diverse metal–oxide supports. Our approach reveals the atomic-scale dynamics of sintering mechanisms and identifies key features of oxide supports governing MSI. We find that the surface energy, surface oxygen bond order, surface dipole and work function of the support are dominant in Pt–oxide interactions. Leveraging these insights, we screened promising sinter-resistant supports for Pt nanoparticles from over 10,000 metal–oxide surfaces and validated some cases by Monte Carlo simulations and experiments. This work integrates iML with NN-MD to accelerate the understanding and discovery of stable supported nanocatalysts, and should be broadly applicable to numerous catalytic applications. The activity and stability of supported metal catalysts is in large part influenced by their interaction with the support. Now, neural network molecular dynamics simulations are combined with interpretable machine learning to reveal the governing factors of metal–support interactions for Pt nanoparticles on various oxide supports, identifying key features and proposing sinter-resistant supports.
{"title":"Predictive model for the discovery of sinter-resistant supports for metallic nanoparticle catalysts by interpretable machine learning","authors":"Chenggong Jiang, Bill Yan, Bryan R. Goldsmith, Suljo Linic","doi":"10.1038/s41929-025-01417-3","DOIUrl":"10.1038/s41929-025-01417-3","url":null,"abstract":"The metal–support interaction (MSI) critically influences the performance of supported nanocatalysts and their long-term stability, yet the factors governing MSIs are multifaceted and challenging to sort out. Here we combine first-principles neural network molecular dynamics (NN-MD) simulations with interpretable machine learning (iML) to shed light on the factors determining MSIs for Pt nanoparticles on diverse metal–oxide supports. Our approach reveals the atomic-scale dynamics of sintering mechanisms and identifies key features of oxide supports governing MSI. We find that the surface energy, surface oxygen bond order, surface dipole and work function of the support are dominant in Pt–oxide interactions. Leveraging these insights, we screened promising sinter-resistant supports for Pt nanoparticles from over 10,000 metal–oxide surfaces and validated some cases by Monte Carlo simulations and experiments. This work integrates iML with NN-MD to accelerate the understanding and discovery of stable supported nanocatalysts, and should be broadly applicable to numerous catalytic applications. The activity and stability of supported metal catalysts is in large part influenced by their interaction with the support. Now, neural network molecular dynamics simulations are combined with interpretable machine learning to reveal the governing factors of metal–support interactions for Pt nanoparticles on various oxide supports, identifying key features and proposing sinter-resistant supports.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1038-1050"},"PeriodicalIF":44.6,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371955","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}
Pub Date : 2025-09-24DOI: 10.1038/s41929-025-01397-4
Valentin Briega-Martos, Rafael Guzman-Soriano, Jiahong Jiang, Yao Yang
Tafel slope analysis, first proposed by Julius Tafel in 1905 and supported by the Butler–Volmer equation, is widely used to elucidate electrocatalytic mechanisms and evaluate kinetics. However, some misuses still frequently occur in the literature, calling for rigorous mechanistic investigations at single-crystal electrodes and under well defined mass-transport conditions.
{"title":"The (mis)uses of Tafel slope","authors":"Valentin Briega-Martos, Rafael Guzman-Soriano, Jiahong Jiang, Yao Yang","doi":"10.1038/s41929-025-01397-4","DOIUrl":"10.1038/s41929-025-01397-4","url":null,"abstract":"Tafel slope analysis, first proposed by Julius Tafel in 1905 and supported by the Butler–Volmer equation, is widely used to elucidate electrocatalytic mechanisms and evaluate kinetics. However, some misuses still frequently occur in the literature, calling for rigorous mechanistic investigations at single-crystal electrodes and under well defined mass-transport conditions.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 9","pages":"863-866"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145129524","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}
Cleavage of hexopyranose to short-chain carbohydrates plays crucial roles in carbon metabolism and energy supply. Currently, the carbon–carbon bond scission of hexopyranose involves two types of reaction: the widely distributed retro-aldol reaction and the transketo-like reaction observed in Bifidobacteria. Here we report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B (ART B), an antibacterial agent from Bacillus. Art22 adopts a TIM-barrel fold, enabling the activation of 4-keto ART B into potent antibiotic ART B via rapid isomerization. In addition, it protects the ART-producing Bacillus by detoxifying cellular ART B to ART B1–B3 via slow oxidative cleavage of the 3-keto hexopyranose to short-chain carbohydrates and CO2. Guided by structural, mutagenic and computational studies, we reveal an anhydride-mediated mechanism for Art22-catalysed oxygenation reactions, which expands the catalytic repertoire of TIM-barrel enzymes and adds an oxidative path for hexopyranose cleavage. Hexopyranose cleavage is a crucial step in carbon metabolism. Here the authors report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B, an antibacterial agent from Bacillus.
六吡喃糖裂解成短链碳水化合物在碳代谢和能量供应中起着至关重要的作用。目前己吡喃糖的碳-碳键断裂涉及两种反应：广泛分布的反醛醇反应和双歧杆菌中观察到的类转酮反应。本文报道了一种新的金属酶Art22的发现和鉴定，该酶参与了来自芽孢杆菌的一种抗菌剂金菌素B （aurantinin B, ART B）的糖段修饰。Art22采用TIM-barrel折叠，通过快速异构化使4-酮类ART B活化为强效抗生素ART B。此外，它通过将3-酮己糖缓慢氧化裂解为短链碳水化合物和二氧化碳，将细胞中的ART B解毒为ART B1-B3，从而保护产生ART的芽胞杆菌。在结构、诱变和计算研究的指导下，我们揭示了一种酸酐介导的art22催化氧化反应机制，这扩大了tim桶酶的催化范围，并增加了六吡喃糖裂解的氧化途径。六吡喃糖的裂解是碳代谢的关键步骤。本文报道了一种新的金属酶Art22的发现和鉴定，该酶参与了金霉素B的糖段修饰。
{"title":"Oxidative cleavage of hexopyranose by a TIM-barrel isomerase","authors":"Pengwei Li, Dacheng Wang, Lu Guo, Yanru Chen, Huijin Mao, Zelian Zhao, Min Wang, Meng Chen, Zhengren Xu, Binju Wang, Defeng Li, Yihua Chen","doi":"10.1038/s41929-025-01412-8","DOIUrl":"10.1038/s41929-025-01412-8","url":null,"abstract":"Cleavage of hexopyranose to short-chain carbohydrates plays crucial roles in carbon metabolism and energy supply. Currently, the carbon–carbon bond scission of hexopyranose involves two types of reaction: the widely distributed retro-aldol reaction and the transketo-like reaction observed in Bifidobacteria. Here we report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B (ART B), an antibacterial agent from Bacillus. Art22 adopts a TIM-barrel fold, enabling the activation of 4-keto ART B into potent antibiotic ART B via rapid isomerization. In addition, it protects the ART-producing Bacillus by detoxifying cellular ART B to ART B1–B3 via slow oxidative cleavage of the 3-keto hexopyranose to short-chain carbohydrates and CO2. Guided by structural, mutagenic and computational studies, we reveal an anhydride-mediated mechanism for Art22-catalysed oxygenation reactions, which expands the catalytic repertoire of TIM-barrel enzymes and adds an oxidative path for hexopyranose cleavage. Hexopyranose cleavage is a crucial step in carbon metabolism. Here the authors report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B, an antibacterial agent from Bacillus.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1010-1022"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371978","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}
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