ArticleProtein science : a publication of the Protein Society2023
New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism.
Article in Protein science : a publication of the Protein Society, 2023. 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, 10 citations in OpenAlex.
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- The binuclear copper state of peptidylglycine monooxygenase visualized through a selenium-substituted peptidyl-homocysteine complex.Dalton transactions (Cambridge, England : 2003) · 2025Article
- How does dopamine convert into norepinephrine? Insights on the key step of the reaction.Journal of molecular modeling · 2025Article
- Peptide Crosslinking by a Class of Plant Copper Enzymes.Trends in chemistry · 2024Article
- Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.Chemical science · 2024Review
- An intramolecular macrocyclase in plant ribosomal peptide biosynthesis.Nature chemical biology · 2024Article
- Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure.Journal of the American Chemical Society · 2024Article
- Ligand-Copper(I) Primary OAccounts of chemical research · 2023Article
- New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Peptidylglycine monooxygenase (PHM) is essential for the biosynthesis of many neuroendocrine peptides via a copper-dependent hydroxylation of a glycine-extended pro-peptide. The "canonical" mechanism requires the transfer of two electrons from one mononuclear copper (CuH, H-site) to a second mononuclear copper (CuM, M-site) which is the site of oxygen binding and catalysis. In most crystal structures the copper centers are separated by 11 Å of disordered solvent, but recent work has established that a PHM variant H108A forms a closed conformer in the presence of citrate with a reduced Cu-Cu site separation of ~4 Å. Here we report three new PHM structures where the H and M sites are separated by a longer distance of ~14 Å. Variation in Cu-Cu distance is the result of a rotation of the M subdomain about a hinge point centered on the pro
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