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Issue 1, 2010
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Resolving ligand hyperfine couplings of type 1 and 2 Cu(II) in ascorbate oxidase by high field pulse EPR correlation spectroscopy

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Abstract

Ascorbate oxidase contains two paramagnetic Cu(II) binding sites, type 1 (T1) and type 2 (T2) and in both sites the Cu(II) is coordinated to histidine residues. We use several pulse EPR techniques at high field (95 GHz) to determine ligand 1H and 14N hyperfine couplings in the two sites and identify the T1 signals by a new triple resonance correlation technique named THYCOS.

Graphical abstract: Resolving ligand hyperfine couplings of type 1 and 2 Cu(ii) in ascorbate oxidase by high field pulse EPR correlation spectroscopy

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Publication details

The article was received on 14 Sep 2009, accepted on 12 Oct 2009 and first published on 07 Nov 2009


Article type: Communication
DOI: 10.1039/B919069D
Citation: Phys. Chem. Chem. Phys., 2010,12, 62-65
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    Resolving ligand hyperfine couplings of type 1 and 2 Cu(II) in ascorbate oxidase by high field pulse EPR correlation spectroscopy

    A. Potapov, I. Pecht and D. Goldfarb, Phys. Chem. Chem. Phys., 2010, 12, 62
    DOI: 10.1039/B919069D

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