{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kato S"],"funding":["Protein Research Foundation","ACT-X","Japan Society for the Promotion of Science"],"pagination":["14837-14844"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12046553"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["147(17)"],"pubmed_abstract":["Cross-coupling reactions between short-lifetime radicals are challenging reactions in organic chemistry. Here, we report the development of an <i>N</i>-heterocyclic carbene (NHC)-mediated radical coupling reaction based on the catalytic machinery of thiamine- and flavin-dependent enzymes. Through a series of enzyme screenings, we found that acetolactate synthase from <i>Thermobispora bispora</i> (TbALS) and its engineered variants exhibit promising catalytic activity toward abiotic radical acylation reactions of α-bromo carbonyl compounds. Notably, the TbALS variant has higher catalytic activity for small nonaromatic substrates despite forming less stable radical intermediates. Furthermore, the catalytic system of TbALS can be applied to photocatalytic reactions utilizing the photoredox pr"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["NHC-Mediated Radical Acylation Catalyzed by Thiamine- and Flavin-Dependent Enzymes."],"pmcid":["PMC12046553"],"funding_grant_id":["JP23H04554","JPMJAX22B6","JP22K21348","JP22H05421","JP24H01136","JP21K05016","JP22K14783","JP24K01630","JP21K20535"],"pubmed_authors":["Shirai T","Mori Y","Bandai M","Hayashi T","Adachi Y","Mori S","Fujisawa S","Kato S"],"additional_accession":[]},"is_claimable":false,"name":"NHC-Mediated Radical Acylation Catalyzed by Thiamine- and Flavin-Dependent Enzymes.","description":"Cross-coupling reactions between short-lifetime radicals are challenging reactions in organic chemistry. Here, we report the development of an <i>N</i>-heterocyclic carbene (NHC)-mediated radical coupling reaction based on the catalytic machinery of thiamine- and flavin-dependent enzymes. Through a series of enzyme screenings, we found that acetolactate synthase from <i>Thermobispora bispora</i> (TbALS) and its engineered variants exhibit promising catalytic activity toward abiotic radical acylation reactions of α-bromo carbonyl compounds. Notably, the TbALS variant has higher catalytic activity for small nonaromatic substrates despite forming less stable radical intermediates. Furthermore, the catalytic system of TbALS can be applied to photocatalytic reactions utilizing the photoredox pr","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-06-01T05:53:19.122Z","creation":"2025-07-08T03:13:28.54Z"},"accession":"S-EPMC12046553","cross_references":{"pubmed":["40232253"],"doi":["10.1021/jacs.5c04484"]}}