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Ligand-Copper(I) Primary O-Adducts: Design, Characterization, and Biological Significance of Cupric-Superoxides.
Acc Chem Res
August 2023
Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, United States.
In this Account, we overview and highlight synthetic bioinorganic chemistry focused on initial adducts formed from the reaction of reduced ligand-copper(I) coordination complexes with molecular oxygen, reactions that produce ligand-Cu(O) complexes (O ≡ superoxide anion). We provide mostly a historical perspective, starting in the Karlin research group in the 1980s, emphasizing the ligand design and ligand effects, structure, and spectroscopy of these O adducts and subsequent further reactivity with substrates, including the interaction with a second ligand-Cu complex to form binuclear species. The Account emphasizes the approach, evolution, and results obtained in the Karlin group, a synthetic bioinorganic research program inspired by the state of knowledge and insights obtained on enzymes possessing copper ion active sites which process molecular oxygen.
View Article and Find Full Text PDFReductive Coupling of Nitric Oxide by Cu(I): Stepwise Formation of Mono- and Dinitrosyl Species to a Cupric Hyponitrite Intermediate.
J Am Chem Soc
February 2023
Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, United States.
Transition-metal-mediated reductive coupling of nitric oxide (NO) to nitrous oxide (NO) has significance across the fields of industrial chemistry, biochemistry, medicine, and environmental health. Herein, we elucidate a density functional theory (DFT)-supplemented mechanism of NO reductive coupling at a copper-ion center, [(tmpa)Cu(MeCN)] () {tmpa = tris(2-pyridylmethyl)amine}. At -110 °C in EtOH (<-90 °C in MeOH), exposing to NO leads to a new binuclear hyponitrite intermediate [{(tmpa)Cu}(μ-NO)] (), exhibiting temperature-dependent irreversible isomerization to the previously characterized κ-O,O'--[(tmpa)Cu(μ-NO)] () complex.
View Article and Find Full Text PDFA Thioether-Ligated Cupric Superoxide Model with Hydrogen Atom Abstraction Reactivity.
J Am Chem Soc
March 2021
Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, United States.
The central role of cupric superoxide intermediates proposed in hormone and neurotransmitter biosynthesis by noncoupled binuclear copper monooxygenases like dopamine-β-monooxygenase has drawn significant attention to the unusual methionine ligation of the Cu ("Cu") active site characteristic of this class of enzymes. The copper-sulfur interaction has proven critical for turnover, raising still-unresolved questions concerning Nature's selection of an oxidizable Met residue to facilitate C-H oxygenation. We describe herein a model for Cu, [(NS)Cu] ([]), and its O-bound analog [(NS)Cu(O)] ([·O]).
View Article and Find Full Text PDFSimplest Monodentate Imidazole Stabilization of the oxy-Tyrosinase Cu2 O2 Core: Phenolate Hydroxylation through a Cu(III) Intermediate.
Angew Chem Int Ed Engl
August 2016
Department of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Tyrosinases are ubiquitous binuclear copper enzymes that oxygenate to Cu(II) 2 O2 cores bonded by three histidine Nτ-imidazoles per Cu center. Synthetic monodentate imidazole-bonded Cu(II) 2 O2 species self-assemble in a near quantitative manner at -125 °C, but Nπ-ligation has been required. Herein, we disclose the syntheses and reactivity of three Nτ-imidazole bonded Cu(II) 2 O2 species at solution temperatures of -145 °C, which was achieved using a eutectic mixture of THF and 2-MeTHF.
View Article and Find Full Text PDFRe-evaluation of the near infrared spectra of mitochondrial cytochrome c oxidase: Implications for non invasive in vivo monitoring of tissues.
Biochim Biophys Acta
November 2014
School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK. Electronic address:
We re-determined the near infrared (NIR) spectral signatures (650-980nm) of the different cytochrome c oxidase redox centres, in the process separating them into their component species. We confirm that the primary contributor to the oxidase NIR spectrum between 700 and 980nm is cupric CuA, which in the beef heart enzyme has a maximum at 835nm. The 655nm band characterises the fully oxidised haem a3/CuB binuclear centre; it is bleached either when one or more electrons are added to the binuclear centre or when the latter is modified by ligands.
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