{"title":"将Ⅰ型醛缩酶重新用于光立体特异性自由基偶联","authors":"Jinhai Yu, Yingdi Hao, Xiaoqiang Huang","doi":"10.1016/j.checat.2024.101191","DOIUrl":null,"url":null,"abstract":"In a recent article published in <em>Nature</em>, Melchiorre and coworkers illuminated enzymatic iminium ions formed through the condensation of 2-deoxyribose-5-phosphate aldolase with enals, triggering photodecarboxylication in the active site, and enabling photoenzymatic stereospecific radical coupling. This elegant work broadens the reactivity of enzymes and achieves a “memory of chirality” scenario.","PeriodicalId":53121,"journal":{"name":"Chem Catalysis","volume":"36 1","pages":""},"PeriodicalIF":11.5000,"publicationDate":"2024-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Repurposing type I aldolase for stereospecific radical coupling with light\",\"authors\":\"Jinhai Yu, Yingdi Hao, Xiaoqiang Huang\",\"doi\":\"10.1016/j.checat.2024.101191\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In a recent article published in <em>Nature</em>, Melchiorre and coworkers illuminated enzymatic iminium ions formed through the condensation of 2-deoxyribose-5-phosphate aldolase with enals, triggering photodecarboxylication in the active site, and enabling photoenzymatic stereospecific radical coupling. This elegant work broadens the reactivity of enzymes and achieves a “memory of chirality” scenario.\",\"PeriodicalId\":53121,\"journal\":{\"name\":\"Chem Catalysis\",\"volume\":\"36 1\",\"pages\":\"\"},\"PeriodicalIF\":11.5000,\"publicationDate\":\"2024-11-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Chem Catalysis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1016/j.checat.2024.101191\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chem Catalysis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/j.checat.2024.101191","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
Repurposing type I aldolase for stereospecific radical coupling with light
In a recent article published in Nature, Melchiorre and coworkers illuminated enzymatic iminium ions formed through the condensation of 2-deoxyribose-5-phosphate aldolase with enals, triggering photodecarboxylication in the active site, and enabling photoenzymatic stereospecific radical coupling. This elegant work broadens the reactivity of enzymes and achieves a “memory of chirality” scenario.
期刊介绍：
Chem Catalysis is a monthly journal that publishes innovative research on fundamental and applied catalysis, providing a platform for researchers across chemistry, chemical engineering, and related fields. It serves as a premier resource for scientists and engineers in academia and industry, covering heterogeneous, homogeneous, and biocatalysis. Emphasizing transformative methods and technologies, the journal aims to advance understanding, introduce novel catalysts, and connect fundamental insights to real-world applications for societal benefit.
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