ArticleBiochemistry2019
Rational Design of a Histidine-Methionine Site Modeling the M-Center of Copper Monooxygenases in a Small Metallochaperone Scaffold.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Unsymmetric bimetallic centres in metalloproteins and synthetic models.Nature reviews. Chemistry · 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
- Mechanisms of Copper Selectivity and Release by the Metallochaperone CusF: Insights from CO-Binding, Rapid-Freeze-Quench EXAFS, and Unnatural Amino Acid Substitution.Inorganic chemistry · 2024Article
- 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
- 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
- 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
- Catalytic M Center of Copper Monooxygenases Probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity.Biochemistry · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Mononuclear copper monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) catalyze the hydroxylation of high energy C-H bonds utilizing a pair of chemically distinct copper sites (CuH and CuM) separated by 11 Å. In earlier work, we constructed single-site PHM variants that were designed to allow the study of the M- and H-centers independently in order to place their reactivity sequentially along the catalytic pathway. More recent crystallographic studies suggest that these single-site variants may not be truly representative of the individual active sites. In this work, we describe an alternative approach that uses a rational design to construct an artificial PHM model in a small metallochaperone scaffold. Using site-directed mutagenesis, we constructed variants that provide a His
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