Resolving ligand hyperfine couplings of type 1 and 2 Cu(II) in ascorbate oxidase by high field pulse EPR correlation spectroscopy.
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 (1)H and (14)N hyperfine couplings in the two sites and identify the T1 signals by a new triple resonance correlation technique named THYCOS.
Potapov
Alexey
A
Department of Chemical Physics, Weizmann Institute of Science, Rehovot Israel 76100.
Pecht
Israel
I
Goldfarb
Daniella
D
D001204:Ascorbate Oxidase / Q000737:chemistry*; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006639:Histidine / Q000737:chemistry; D008024:Ligands
D008024:Ligands; D006639:Histidine; D003300:Copper; D001204:Ascorbate Oxidase