ArticleJournal of the American Chemical Society2015
A "naked" Fe(III)-(O₂²⁻)-Cu(II) species allows for structural and spectroscopic tuning of low-spin heme-peroxo-Cu complexes.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Modulation of heme peroxo nucleophilicities with axial ligands reveal key insights into the mechanistic landscape of nitric oxide synthase.Chemical science · 2025Article
- Reactivity of a heterobinuclear heme-peroxo-Cu complex withChemical science · 2025Article
- A Bioinspired Nonheme FeJournal of the American Chemical Society · 2024Article
- Heme-copper and Heme OJournal of inorganic biochemistry · 2023Review
- Isolating Fe-OMolecules (Basel, Switzerland) · 2022Review
- Using a monocopper-superoxo complex to prepare multicopper-peroxo species relevant to proposed enzyme intermediates.Journal of inorganic biochemistry · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Heme-Cu Binucleating Ligand Supports Heme/OInorganic chemistry · 2019Article
- Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in CytochromeJournal of the American Chemical Society · 2019Article
- Spin Interconversion of Heme-Peroxo-Copper Complexes Facilitated by Intramolecular Hydrogen-Bonding Interactions.Journal of the American Chemical Society · 2019Article
- Influence of intramolecular secondary sphere hydrogen-bonding interactions on cytochromeChemical science · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Chemical reviews · 2018Review
- Phenol-Induced O-O Bond Cleavage in a Low-Spin Heme-Peroxo-Copper Complex: Implications for OJournal of the American Chemical Society · 2017Article
- Activation of dioxygen by copper metalloproteins and insights from model complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.Journal of the American Chemical Society · 2017Article
- Isocyanide or nitrosyl complexation to hemes with varying tethered axial base ligand donors: synthesis and characterization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- A broken-symmetry density functional study of structures, energies, and protonation states along the catalytic O-O bond cleavage pathway in ba3 cytochrome c oxidase from Thermus thermophilus.Physical chemistry chemical physics : PCCP · 2016Article
- Nitric oxide activation by distal redox modulation in tetranuclear iron nitrosyl complexes.Journal of the American Chemical Society · 2015Article
- Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a "Bridging Peroxo" Intermediate Involved in Facile 4e(-)/4H(+) O2-Reduction.Journal of the American Chemical Society · 2015Article
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Abstract
Here we describe a new approach for the generation of heme-peroxo-Cu compounds, using a "naked" complex synthon, [(F8)Fe(III)-(O2(2-))-Cu(II)(MeTHF)3](+) (MeTHF = 2-methyltetrahydrofuran; F8 = tetrakis(2,6-difluorophenyl)porphyrinate). Addition of varying ligands (L) for Cu allows the generation and spectroscopic characterization of a family of high- and low-spin Fe(III)-(O2(2-))-Cu(II)(L) complexes. These possess markedly varying Cu(II) coordination geometries, leading to tunable Fe-O, O-O, and Cu-O bond strengths. DFT calculations accompanied by vibrational data correlations give detailed structural insights.
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