{"doi":"10.1021/jacs.4c04402","title":"Intramolecular Phenolic H-Atom Abstraction by a N<sub>3</sub>ArOH Ligand-Supported (μ-η<sup>2</sup>:η<sup>2</sup>-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase","abstract":"Synthetic side-on peroxide-bound dicopper(II) ( S P ) complexes are important for understanding the active site structure/function of many copper-containing enzymes. This work highlights the formation of new {Cu II (μ-η 2:η 2 -O 2 2– )Cu II } complexes (with electronic absorption and resonance Raman (rR) spectroscopic characterization) using tripodal N 3 ArOH ligands at −135 °C, which spontaneously participate in intramolecular phenolic H-atom abstraction (HAA). This results in the generation of bis(phenoxyl radical)bis(μ-OH)dicopper(II) intermediates, substantiated by their EPR/UV–vis/rR spectroscopic signatures and crystal structural determination of a diphenoquinone dicopper(I) complex derived from ligand para -C═C coupling. The newly observed chemistry in these ligand–Cu systems is discussed with respect to (a) our Cu-MeAN (tridentate N, N, N ′, N ′, N ″-pentamethyldipropylenetriamine)-derived model S P species, which was unreactive toward exogenous monophenol addition ( J . Am . Chem . Soc . 2012, 134, 8513–8524), emphasizing the impact of intramolecularly tethered ArOH groups, and (b) recent advances in understanding the mechanism of action of the tyrosinase (Ty) enzyme.","journal":"Journal of the American Chemical Society","year":2024,"id":462982,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":7,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9577,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2024-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1087508,"name":"Hai Phan","orcid":"0009-0004-9233-5496","position":1,"is_corresponding":false},{"id":1067454,"name":"Eleanor M. Dunietz","orcid":"0009-0005-0544-3825","position":2,"is_corresponding":false},{"id":1026986,"name":"Magdalene T. Brueggemeyer","orcid":"0000-0002-0205-8033","position":3,"is_corresponding":false},{"id":981286,"name":"Pradip Kumar Hota","orcid":"0000-0002-1502-4879","position":4,"is_corresponding":false},{"id":414296,"name":"Maxime A. Siegler","orcid":"0000-0003-4165-7810","position":5,"is_corresponding":false},{"id":786873,"name":"Anex Jose","orcid":"0000-0002-4924-7886","position":6,"is_corresponding":false},{"id":414295,"name":"Mayukh Bhadra","orcid":"0000-0002-4758-1610","position":7,"is_corresponding":false},{"id":271050,"name":"Edward I. Solomon","orcid":"0000-0003-0291-3199","position":8,"is_corresponding":false},{"id":414300,"name":"Kenneth D. Karlin","orcid":"0000-0002-5675-7040","position":9,"is_corresponding":false},{"id":1087507,"name":"Sanjib Panda","orcid":"0000-0001-6556-8009","position":0,"is_corresponding":true}],"reference_count":48,"raw_metadata":null,"created_at":"2026-07-19T02:04:28.838123Z","pmid":"38775712","pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}