Nature Catalysis Nature Catalysis brings together researchers from across all chemistry and related fields, publishing work on homogeneous catalysis, heterogeneous catalysis, and biocatalysts, incorporating both fundamental and applied studies. We have a particular interest in applied work that advances our knowledge and informs the development of sustainable industries and processes. Nature Catalysis provides coverage of the science and business of catalysis research, creating a unique journal for scientists, engineers and researchers in academia and industry. http://feeds.nature.com/natcatal/rss/current Nature Publishing Group en © 2025 Macmillan Publishers Limited, part of Springer Nature. All rights reserved. Nature Catalysis © 2025 Macmillan Publishers Limited, part of Springer Nature. All rights reserved. [email protected]
  • Nature Catalysis https://www.nature.com/uploads/product/natcatal/rss.png http://feeds.nature.com/natcatal/rss/current <![CDATA[Copper-catalysed homo-Mannich reaction of cyclopropanol for chiral piperidine synthesis]]> https://www.nature.com/articles/s41929-025-01432-4 <![CDATA[
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    Nature Catalysis, Published online: 24 October 2025; doi:10.1038/s41929-025-01432-4

    The Mannich reaction has long been used by chemists for the synthesis of stereoselective synthesis of β-amino-carbonyl compounds. Here, the authors show a catalytic homo-Mannich reaction of cyclopropanols with in situ-formed imines, furnishing chiral 2,6-disubstituted piperidines in good yields with high diastereoselectivities due to the use of a diketiminate-complexed copper.]]> <![CDATA[Copper-catalysed homo-Mannich reaction of cyclopropanol for chiral piperidine synthesis]]> Yankun ZhaoWenxuan LinYulian ZhangGuangcheng PuZhuoyuan JianHongya YanLing HeChengyang WangQiuyuan TanYu LanMin Zhang doi:10.1038/s41929-025-01432-4 Nature Catalysis, Published online: 2025-10-24; | doi:10.1038/s41929-025-01432-4 2025-10-24 Nature Catalysis 10.1038/s41929-025-01432-4 https://www.nature.com/articles/s41929-025-01432-4 <![CDATA[Selection for photocatalytic function through Darwinian evolution of synthetic self-replicators]]> https://www.nature.com/articles/s41929-025-01409-3 <![CDATA[

    Nature Catalysis, Published online: 24 October 2025; doi:10.1038/s41929-025-01409-3

    Darwinian evolution has shaped life on our planet through natural selection. Here, the authors report on the combination of self-replication, mutation and protometabolism in an out-of-equilibrium abiotic chemical system that can lead to natural selection for protometabolic activity.]]>     <![CDATA[Selection for photocatalytic function through Darwinian evolution of synthetic self-replicators]]> Kai LiuOmer MarkovitchChris van EwijkYari Katar KnelissenArmin KianiMarcel EleveldWouter H. RoosSijbren Otto doi:10.1038/s41929-025-01409-3 Nature Catalysis, Published online: 2025-10-24; | doi:10.1038/s41929-025-01409-3 2025-10-24 Nature Catalysis 10.1038/s41929-025-01409-3 https://www.nature.com/articles/s41929-025-01409-3     <![CDATA[Silicon frustrated Lewis pairs catalyse α-deuteration of amides and esters]]> https://www.nature.com/articles/s41929-025-01420-8 <![CDATA[

    Nature Catalysis, Published online: 24 October 2025; doi:10.1038/s41929-025-01420-8

    Deuterated bioactive compounds are important as diagnostic tools and pharmaceuticals, but current methods of development are limited. Here the authors report how a silicon Lewis acid and a tertiary amine base act as a frustrated Lewis pair to catalyse the hydrogen exchange reaction for the deuteration of amides and esters.]]>     <![CDATA[Silicon frustrated Lewis pairs catalyse α-deuteration of amides and esters]]> Y. KogaI. FukumotoK. MasuiT. TanakaY. NaganawaM. HayashiT. OhshimaR. Yazaki doi:10.1038/s41929-025-01420-8 Nature Catalysis, Published online: 2025-10-24; | doi:10.1038/s41929-025-01420-8 2025-10-24 Nature Catalysis 10.1038/s41929-025-01420-8 https://www.nature.com/articles/s41929-025-01420-8     <![CDATA[Enantioselective energy transfer catalysis compartmentalized by triplet photoenzymes]]> https://www.nature.com/articles/s41929-025-01433-3 <![CDATA[

    Nature Catalysis, Published online: 24 October 2025; doi:10.1038/s41929-025-01433-3

    Artificial photobiocatalytic reactions are appealing but sometimes suffer from non-enzymatic side reactions. Now a photoenzyme for enantioselective [2 + 2] photocycloaddition of 2-naphthyl derivatives is reported and combined with designed quenchers that shut down the competing enzyme-free racemic reaction.]]>     <![CDATA[Enantioselective energy transfer catalysis compartmentalized by triplet photoenzymes]]> Xinjie YangJuan GuoJunyi QianJianjian HuangJuan ShiMiao JiangJunshuai ZhangTengfei PangNingning SunYu FuWeining ZhaoGuojiao WuXi ChenYuzhou WuFangrui Zhong doi:10.1038/s41929-025-01433-3 Nature Catalysis, Published online: 2025-10-24; | doi:10.1038/s41929-025-01433-3 2025-10-24 Nature Catalysis 10.1038/s41929-025-01433-3 https://www.nature.com/articles/s41929-025-01433-3     <![CDATA[Architecture, catalysis and regulation of methylthio-alkane reductase for bacterial sulfur acquisition from volatile organic compounds]]> https://www.nature.com/articles/s41929-025-01425-3 <![CDATA[

    Nature Catalysis, Published online: 23 October 2025; doi:10.1038/s41929-025-01425-3

    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.]]>     <![CDATA[Architecture, catalysis and regulation of methylthio-alkane reductase for bacterial sulfur acquisition from volatile organic compounds]]> Srividya MuraliGuo-Bin HuDale F. KreitlerAna Arroyo CarriedoLuke C. LewisSamuel Adu FosuOlivia G. WeaverElla M. BuzasKathryn M. ByerlyYasuo YoshikuniSean McSweeneyHannah S. ShafaatJustin A. North doi:10.1038/s41929-025-01425-3 Nature Catalysis, Published online: 2025-10-23; | doi:10.1038/s41929-025-01425-3 2025-10-23 Nature Catalysis 10.1038/s41929-025-01425-3 https://www.nature.com/articles/s41929-025-01425-3     <![CDATA[Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage]]> https://www.nature.com/articles/s41929-025-01426-2 <![CDATA[

    Nature Catalysis, Published online: 23 October 2025; doi:10.1038/s41929-025-01426-2

    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.]]>     <![CDATA[Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage]]> Ana Lago-MacielJéssica C. SoaresJan ZarzyckiCharles J. BuchananTristan Reif-TrauttmansdorffFrederik V. SchmidtStefano LomettoNicole PacziaJan M. SchullerD. Flemming HansenGabriella T. HellerSimone PrinzGeorg K. A. HochbergAntonio J. PierikJohannes G. Rebelein doi:10.1038/s41929-025-01426-2 Nature Catalysis, Published online: 2025-10-23; | doi:10.1038/s41929-025-01426-2 2025-10-23 Nature Catalysis 10.1038/s41929-025-01426-2 https://www.nature.com/articles/s41929-025-01426-2     <![CDATA[Electrolyte effects in proton–electron transfer reactions and implications for renewable fuels and chemicals synthesis]]> https://www.nature.com/articles/s41929-025-01421-7 <![CDATA[

    Nature Catalysis, Published online: 23 October 2025; doi:10.1038/s41929-025-01421-7

    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.]]>     <![CDATA[Electrolyte effects in proton–electron transfer reactions and implications for renewable fuels and chemicals synthesis]]> Paula Sebastián-PascualAntonia HerzogYirui ZhangYang Shao-HornMaría Escudero-Escribano doi:10.1038/s41929-025-01421-7 Nature Catalysis, Published online: 2025-10-23; | doi:10.1038/s41929-025-01421-7 2025-10-23 Nature Catalysis 10.1038/s41929-025-01421-7 https://www.nature.com/articles/s41929-025-01421-7     <![CDATA[Determining CO adsorption free energies on CO<sub>2</sub> electroreduction active sites through kinetic analysis]]> https://www.nature.com/articles/s41929-025-01427-1 <![CDATA[

    Nature Catalysis, Published online: 23 October 2025; doi:10.1038/s41929-025-01427-1

    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.]]>     <![CDATA[Determining CO adsorption free energies on CO<sub>2</sub> electroreduction active sites through kinetic analysis]]> Zhihao CuiKassidy D. AztergoJiseon HwangAnne C. Co doi:10.1038/s41929-025-01427-1 Nature Catalysis, Published online: 2025-10-23; | doi:10.1038/s41929-025-01427-1 2025-10-23 Nature Catalysis 10.1038/s41929-025-01427-1 https://www.nature.com/articles/s41929-025-01427-1