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Oxygen Delivery as a Limiting Factor in Modelling Dicopper(II) Oxidase Reactivity

  • Deprotonation of ligand-appended alkoxyl groups in mononuclear copper(II) complexes of N,O ligands L-1 and L-2, gave dinuclear complexes sharing symmetrical Cu2O2 cores. Molecular structures of these mono-and binuclear complexes have been characterized by XRD, and their electronic structures by UV/Vis, H-1 NMR, EPR and DFT; moreover, catalytic performance as models of catechol oxidase was studied. The binuclear complexes with anti-ferromagnetically coupled copper(II) centers are moderately active in quinone formation from 3,5-di-tert-butyl-catechol under the estab-lished conditions of oxygen saturation, but are strongly activated when additional dioxygen is administered during catalytic turnover. This unforeseen and unprecedented effect is attributed to increased maximum reaction rates v(max), whereas the substrate affinity KM remains unaffected. Oxygen administration is capable of (partially) removing limitations to turnover caused by product inhibition. Because product inhibition is generally accepted to be a major limitation ofDeprotonation of ligand-appended alkoxyl groups in mononuclear copper(II) complexes of N,O ligands L-1 and L-2, gave dinuclear complexes sharing symmetrical Cu2O2 cores. Molecular structures of these mono-and binuclear complexes have been characterized by XRD, and their electronic structures by UV/Vis, H-1 NMR, EPR and DFT; moreover, catalytic performance as models of catechol oxidase was studied. The binuclear complexes with anti-ferromagnetically coupled copper(II) centers are moderately active in quinone formation from 3,5-di-tert-butyl-catechol under the estab-lished conditions of oxygen saturation, but are strongly activated when additional dioxygen is administered during catalytic turnover. This unforeseen and unprecedented effect is attributed to increased maximum reaction rates v(max), whereas the substrate affinity KM remains unaffected. Oxygen administration is capable of (partially) removing limitations to turnover caused by product inhibition. Because product inhibition is generally accepted to be a major limitation of catechol oxidase models, we think that our observations will be applicable more widely.show moreshow less

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Metadaten
Author details:Jana Guelzow, Gerald HoernerORCiD, Peter StrauchGND, Anika Stritt, Elisabeth Irran, Andreas Grohmann
DOI:https://doi.org/10.1002/chem.201605868
ISSN:0947-6539
ISSN:1521-3765
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/28094884
Title of parent work (English):Chemistry - a European journal
Publisher:Wiley-VCH
Place of publishing:Weinheim
Publication type:Article
Language:English
Year of first publication:2017
Publication year:2017
Release date:2020/04/20
Volume:23
Number of pages:15
First page:7009
Last Page:7023
Funding institution:Deutsche Forschungsgemeinschaft (DFG) [GR 1247/7-1, SFB 658]
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer review:Referiert
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