ArticleJournal of the American Chemical Society2024
Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Emerging classes of copper enzymes.Current opinion in chemical biology · 2026Review
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- Recent Advances in Bioinspired Cu-Directed C-H Hydroxylation Reactions.Accounts of chemical research · 2025Article
- Copper-Dependent Hydroxylation Catalyzed by the DUF3328 Enzyme CctR.Organic letters · 2025Article
- The binuclear copper state of peptidylglycine monooxygenase visualized through a selenium-substituted peptidyl-homocysteine complex.Dalton transactions (Cambridge, England : 2003) · 2025Article
- Peptide Crosslinking by a Class of Plant Copper Enzymes.Trends in chemistry · 2024Article
- Expanding the Clip-and-Cleave Concept: Approaching Enantioselective C-H Hydroxylations by Copper Imine Complexes Using OJournal of the American Chemical Society · 2024Article
- A Four-Coordinate End-On Superoxocopper(II) Complex: Probing the Link between Coordination Number and Reactivity.Journal of the American Chemical Society · 2024Article
- Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.Chemical science · 2024Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Peptidylglycine monooxygenase is a copper-dependent enzyme that catalyzes C-alpha hydroxylation of glycine extended pro-peptides, a critical post-translational step in peptide hormone processing. The canonical mechanism posits that dioxygen binds at the mononuclear M-center to generate a Cu(II)-superoxo species capable of H atom abstraction from the peptidyl substrate, followed by long-range electron tunneling from the CuH center. Recent crystallographic and biochemical data have challenged this mechanism, suggesting instead that an "open-to-closed" transition brings the copper centers closer, allowing reactivity within a binuclear intermediate. Here we present the first direct observation of an enzyme-bound binuclear copper species, captured by the use of an Ala-Ala-Phe-hCys inhibitor complex. This molecule reacts with the fully reduced enzyme to form a thiolate-bridged binuclear species characterized by EXAFS of the WT and its M314H variant and with the oxidized enzyme to form a novel mixed valence entity characterized by UV/vis and EPR. Mechanistic implications are discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.