ReviewInorganic chemistry2016
Dioxygen Binding, Activation, and Reduction to H2O by Cu Enzymes.
Review in Inorganic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 67 citations in OpenAlex.
- Remolding laccase for whole-cell and in vivo modulation of dopamine signal.Science advances · 2025Article
- How does dopamine convert into norepinephrine? Insights on the key step of the reaction.Journal of molecular modeling · 2025Article
- Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.Chemical science · 2024Review
- A supramolecular metalloenzyme possessing robust oxidase-mimetic catalytic function.Nature communications · 2023Article
- Antisymmetric Spin Exchange in a μ-1,2-Peroxodicopper(II) Complex with an Orthogonal Cu-O-O-Cu Arrangement andJACS Au · 2022Article
- Tuning metal-metal interactions for cooperative small molecule activation.Chemical communications (Cambridge, England) · 2021Review
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Iron and manganese oxo complexes, oxo wall and beyond.Nature reviews. Chemistry · 2020Review
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- The teleos of metallo-reduction and metallo-oxidation in eukaryotic iron and copper trafficking.Metallomics : integrated biometal science · 2018Article
- A High-Valent Non-Heme μ-Oxo Manganese(IV) Dimer Generated from a Thiolate-Bound Manganese(II) Complex and Dioxygen.Angewandte Chemie (International ed. in English) · 2017Article
- Acid/base triggered interconversion of μ-ηChemical science · 2017Article
- Copper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.Chemical reviews · 2017Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Oxygen intermediates in copper enzymes exhibit unique spectroscopic features that reflect novel geometric and electronic structures that are key to reactivity. This perspective will describe: (1) the bonding origin of the unique spectroscopic features of the coupled binuclear copper enzymes and how this overcomes the spin forbiddenness of O2 binding and activates monooxygenase activity, (2) how the difference in exchange coupling in the non-coupled binuclear Cu enzymes controls the reaction mechanism, and (3) how the trinuclear Cu cluster present in the multicopper oxidases leads to a major structure/function difference in enabling the irreversible reductive cleavage of the O-O bond with little overpotential and generating a fully oxidized intermediate, different from the resting enzyme studied by crystallography, that is key in enabling fast PCET in the reductive half of the catalytic cycle.
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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.