{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rush KW"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["5074-5080"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11096088"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146(8)"],"pubmed_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 com"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure."],"pmcid":["PMC11096088"],"funding_grant_id":["R35 GM126956","P30 GM133894","R35 GM136239","R35GM126956","1R35GM136239","T32 GM122740"],"pubmed_authors":["Eastman KAS","Welch EF","Bandarian V","Blackburn NJ","Rush KW"],"additional_accession":[]},"is_claimable":false,"name":"Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure.","description":"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 com","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2026-06-02T19:12:58.664Z","creation":"2025-04-20T01:48:09.174Z"},"accession":"S-EPMC11096088","cross_references":{"pubmed":["38363651"],"doi":["10.1021/jacs.3c14705"]}}