{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chiang CY"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["126-132"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12145154"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["638(8049)"],"pubmed_abstract":["Carbon-hydrogen (C-H) bonds are the foundation of essentially every organic molecule, making them an ideal place to do chemical synthesis. The key challenge is achieving selectivity for one particular C(sp<sup>3</sup>)-H bond<sup>1-3</sup>. In recent years, metalloenzymes have been found to perform C(sp<sup>3</sup>)-H bond functionalization<sup>4,5</sup>. Despite substantial progresses in the past two decades<sup>6,7</sup>, enzymatic halogenation and pseudohalogenation of unactivated C(sp<sup>3</sup>)-H-providing a functional handle for further modification-have been achieved with only non-haem iron/α-ketoglutarate-dependent halogenases, and are therefore limited by the chemistry possible with these enzymes<sup>8</sup>. Here we report the discovery and characterization of a previously unkn"],"journal":["Nature"],"pubmed_title":["Copper-dependent halogenase catalyses unactivated C-H bond functionalization."],"pmcid":["PMC12145154"],"funding_grant_id":["R35 GM150762","R01 AI141481","R35 GM118056","R35 GM145286"],"pubmed_authors":["Zhou Q","Guo Y","Le J","Ohashi M","Chen PP","Houk KN","Hematian S","Bat-Erdene U","Qu S","Rodriguez JA","Loo JA","Chiang CY","Tang Y"],"additional_accession":[]},"is_claimable":false,"name":"Copper-dependent halogenase catalyses unactivated C-H bond functionalization.","description":"Carbon-hydrogen (C-H) bonds are the foundation of essentially every organic molecule, making them an ideal place to do chemical synthesis. The key challenge is achieving selectivity for one particular C(sp<sup>3</sup>)-H bond<sup>1-3</sup>. In recent years, metalloenzymes have been found to perform C(sp<sup>3</sup>)-H bond functionalization<sup>4,5</sup>. Despite substantial progresses in the past two decades<sup>6,7</sup>, enzymatic halogenation and pseudohalogenation of unactivated C(sp<sup>3</sup>)-H-providing a functional handle for further modification-have been achieved with only non-haem iron/α-ketoglutarate-dependent halogenases, and are therefore limited by the chemistry possible with these enzymes<sup>8</sup>. Here we report the discovery and characterization of a previously unkn","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-03-18T13:29:21.721Z","creation":"2025-08-18T09:54:10.971Z"},"accession":"S-EPMC12145154","cross_references":{"pubmed":["39880944"],"doi":["10.1038/s41586-024-08362-4"]}}