{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ochs J"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["4183-4190"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12777740"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(8)"],"pubmed_abstract":["Similar to Pt<sup>IV</sup> prodrugs, Au<sup>III</sup> anticancer complexes are believed to undergo intracellular reduction, thereby gaining their activity from the resulting Au<sup>I</sup> species. Unlike for Pt<sup>IV</sup>, the underlying mechanism of this process remains poorly understood for Au<sup>III</sup>. To elucidate this mechanism, we investigated the reaction of [Au(ppy)Cl<sub>2</sub>], a model Au<sup>III</sup> complex (ppy: phenylpyridine), with two biologically relevant reductants: lipoic acid (lpa) and <i>N</i>-acetyl-l-cysteine-methyl ester (NAC-OMe). Our findings reveal that lpa transfers a hydride to the Au, while cysteine derivatives only bind to the metal. The Au-H complex, even visible in protic solvents by NMR spectroscopy, produced by lpa is essential for enabling a s"],"journal":["Chemical science"],"pubmed_title":["Identification of Au-hydrides as key intermediates in the reduction of Au(iii) prodrugs to active Au(i) species under protic conditions."],"pmcid":["PMC12777740"],"funding_grant_id":["GRK 2341 “Microbial Substrate Conversion”"],"pubmed_authors":["Metzler-Nolte N","Ochs J"],"additional_accession":[]},"is_claimable":false,"name":"Identification of Au-hydrides as key intermediates in the reduction of Au(iii) prodrugs to active Au(i) species under protic conditions.","description":"Similar to Pt<sup>IV</sup> prodrugs, Au<sup>III</sup> anticancer complexes are believed to undergo intracellular reduction, thereby gaining their activity from the resulting Au<sup>I</sup> species. Unlike for Pt<sup>IV</sup>, the underlying mechanism of this process remains poorly understood for Au<sup>III</sup>. To elucidate this mechanism, we investigated the reaction of [Au(ppy)Cl<sub>2</sub>], a model Au<sup>III</sup> complex (ppy: phenylpyridine), with two biologically relevant reductants: lipoic acid (lpa) and <i>N</i>-acetyl-l-cysteine-methyl ester (NAC-OMe). Our findings reveal that lpa transfers a hydride to the Au, while cysteine derivatives only bind to the metal. The Au-H complex, even visible in protic solvents by NMR spectroscopy, produced by lpa is essential for enabling a s","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T21:26:13.256Z","creation":"2026-07-10T03:16:03.167Z"},"accession":"S-EPMC12777740","cross_references":{"pubmed":["41510013"],"doi":["10.1039/d5sc06212h"]}}