ArticleCommunications biology2018
Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase.
Article in Communications biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- 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
- Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure.Journal of the American Chemical Society · 2024Article
- Transition metal ions and neurotransmitters: coordination chemistry and implications for neurodegeneration.RSC chemical biology · 2023Review
- 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
- Peptidylglycine α-amidating monooxygenase as a therapeutic target or biomarker for human diseases.British journal of pharmacology · 2022Review
- Copper monooxygenase reactivity: Do consensus mechanisms accurately reflect experimental observations?Journal of inorganic biochemistry · 2022Article
- Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate Triggering of the Active Conformer.Biochemistry · 2022Article
- Review
- Copper and the brain noradrenergic system.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Review
- Cilia-based peptidergic signaling.PLoS biology · 2019Article
- Catalytic M Center of Copper Monooxygenases Probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity.Biochemistry · 2019Article
- Rational Design of a Histidine-Methionine Site Modeling the M-Center of Copper Monooxygenases in a Small Metallochaperone Scaffold.Biochemistry · 2019Article
- Getting the Most Out of Your Crystals: Data Collection at the New High-Flux, Microfocus MX Beamlines at NSLS-II.Molecules (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The structures of metalloproteins that use redox-active metals for catalysis are usually exquisitely folded in a way that they are prearranged to accept their metal cofactors. Peptidylglycine α-hydroxylating monooxygenase (PHM) is a dicopper enzyme that catalyzes hydroxylation of the α-carbon of glycine-extended peptides for the formation of des-glycine amidated peptides. Here, we present the structures of apo-PHM and of mutants of one of the copper sites (H107A, H108A, and H172A) determined in the presence and absence of citrate. Together, these structures show that the absence of one copper changes the conformational landscape of PHM. In one of these structures, a large interdomain rearrangement brings residues from both copper sites to coordinate a single copper (closed conformation) indicating that full copper occupancy is necessary for locking the catalytically competent conformation (open). These data suggest that in addition to their required participation in catalysis, the redox-active metals play an important structural role.
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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.