ArticleJournal of the American Chemical Society2008
Inner-sphere mechanism for molecular oxygen reduction catalyzed by copper amine oxidases.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 66 citations in OpenAlex.
- Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase.Chemical science · 2022Article
- Aldehyde catalysis - from simple aldehydes to artificial enzymes.RSC advances · 2020Review
- Molecular mechanism of the chitinolytic peroxygenase reaction.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Characterization of the Preprocessed Copper Site Equilibrium in Amine Oxidase and Assignment of the Reactive Copper Site in Topaquinone Biogenesis.Journal of the American Chemical Society · 2019Article
- Co(II) is not oxidized during turnover in the copper amine oxidase from Hansenula polymorpha.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Copper amine oxidases catalyze the oxidative deamination and hydrolysis of cyclic imines.Nature communications · 2019Article
- Targeted quantitative profiling of metabolites and gene transcripts associated with 4-aminobutyrate (GABA) in apple fruit stored under multiple abiotic stresses.Horticulture research · 2018Article
- Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis.Biochemistry · 2016Article
- Probing the Catalytic Mechanism of Copper Amine Oxidase from Arthrobacter globiformis with Halide Ions.The Journal of biological chemistry · 2015Article
- Lewis acid-induced change from four- to two-electron reduction of dioxygen catalyzed by copper complexes using scandium triflate.Journal of the American Chemical Society · 2015Article
- Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.Chemical reviews · 2014Review
- Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase.FEBS letters · 2014Article
- Structural snapshots from the oxidative half-reaction of a copper amine oxidase: implications for O2 activation.The Journal of biological chemistry · 2013Article
- Temperature-independent catalytic two-electron reduction of dioxygen by ferrocenes with a copper(II) tris[2-(2-pyridyl)ethyl]amine catalyst in the presence of perchloric acid.Journal of the American Chemical Society · 2013Article
- Factors that control catalytic two- versus four-electron reduction of dioxygen by copper complexes.Journal of the American Chemical Society · 2012Article
- Cobalt substitution supports an inner-sphere electron transfer mechanism for oxygen reduction in pea seedling amine oxidase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase.International journal of molecular sciences · 2012Article
- Characterization of a protein-generated O₂ binding pocket in PqqC, a cofactorless oxidase catalyzing the final step in PQQ production.Biochemistry · 2011Article
- CO and O2 binding to pseudo-tetradentate ligand-copper(I) complexes with a variable N-donor moiety: kinetic/thermodynamic investigation reveals ligand-induced changes in reaction mechanism.Journal of the American Chemical Society · 2010Article
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7 authors at 2 institutions in 1 country.
Funding
Abstract
Copper and topaquinone (TPQ) containing amine oxidases utilize O2 for the metabolism of biogenic amines while concomitantly generating H2O2 for use by the cell. The mechanism of O2 reduction has been the subject of long-standing debate due to the obscuring influence of a proton-coupled electron transfer between the tyrosine-derived TPQ and copper, a rapidly established equilibrium precluding assignment of the enzyme in its reactive form. Here, we show that substrate-reduced pea seedling amine oxidase (PSAO) exists predominantly in the Cu(I), TPQ semiquinone state. A new mechanistic proposal for O2 reduction is advanced on the basis of thermodynamic considerations together with kinetic studies (at varying pH, temperature, and viscosity), the identification of steady-state intermediates, and the analysis of competitive oxygen kinetic isotope effects, (18)O KIEs, [kcat/KM((16,16)O2)]/[kcat/KM((16,18)O2)]. The (18)O KIE = 1.0136 +/- 0.0013 at pH 7.2 is independent of temperature from 5 degrees C to 47 degrees C and insignificantly changed to 1.0122 +/- 0.0020 upon raising the pH to 9, thus indicating the absence of kinetic complexity. Using density functional methods, the effect is found to be precisely in the range expected for reversible O2 binding to Cu(I) to afford a superoxide, [Cu(II)(eta(1)-O2)(-I)](+), intermediate. Electron transfer from the TPQ semiquinone follows in the first irreversible step to form a peroxide, Cu(II)(eta(1)-O2)(-II), intermediate driving the reduction of O2. The similar (18)O KIEs reported for copper amine oxidases from other sources raise the possibility that all enzymes react by related inner-sphere mechanisms although additional experiments are needed to test this proposal.
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