1.10.3.3 Co2+ contains copper 742708 1.10.3.3 copper - 439890, 439912, 439928, 439932 1.10.3.3 copper 10 copper atoms per enzyme molecule 439890 1.10.3.3 copper 10-12 atoms of copper per enzyme molecule of 140000 Da 439896 1.10.3.3 copper 4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3 439899 1.10.3.3 copper 8 atoms of copper per enzyme molecule of 132000 Da 439894 1.10.3.3 copper 8 atoms of copper per enzyme molecule of 140000 Da 439895, 439904, 439922 1.10.3.3 copper a multicopper protein, 6 atoms of copper per enzyme molecule 439889 1.10.3.3 copper coordination environment of type 2 copper 439915 1.10.3.3 copper each subunit has 4 copper atoms bound as mononuclear and trinuclear species, mononuclear copper representing the type I copper is located in the 3 domain 439902 1.10.3.3 copper electronic structure of blue copper sites 439914 1.10.3.3 copper enzyme contains a set of 1 type I, 1 type II and a pair of type III copper ions at its active site 439917 1.10.3.3 copper enzyme contains type I, type II and type III copper atoms in the ratio 1/2/2, 4 copper atoms/enzyme 439929 1.10.3.3 copper evidence that the coordination environment and electronic structure of the type 1 copper is similar to those of plastocyanin and azurin 439914 1.10.3.3 copper measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme 439900 1.10.3.3 copper multi-copper oxidase 764908 1.10.3.3 copper native enzyme contains two type 1, two type 2 and four type 3 copper ions 439904 1.10.3.3 copper principal active site comprised of one type I, one type II and a pair of type III coppers 439917 1.10.3.3 copper the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate 684895 1.10.3.3 copper type 2 copper may be part of the ascorbate binding site 439915 1.10.3.3 copper type I and trinuclear type II copper center 656442 1.10.3.3 Cu2+ - 717286 1.10.3.3 Cu2+ 9 copper atoms per enzyme molecule. Each subunit has four copper atoms bound as mononuclear and trinuclear species. The mononuclear copper has two histidine, a cysteine and a methionine ligand and represents the type-l copper. It is located in domain 3. Binding structure analysis, copper site structures, detailed overview 717986 1.10.3.3 Cu2+ a blue copper-containing oxidase 676487 1.10.3.3 Cu2+ a multicopper oxidase 724853 1.10.3.3 Cu2+ a multicopper oxidase, contains type 1 Cu2+, binding residues are His445, Cys507, His512, and Met517 673049 1.10.3.3 Cu2+ a plant blue-copper protein 675660 1.10.3.3 Cu2+ copper-containing enzyme 676728 1.10.3.3 Cu2+ essential for activity, a tri-nuclear copper center structure, a partial loss of tertiary structure has strong effects on copper 673569 1.10.3.3 additional information no support of a metal in the enzyme 396331 1.10.3.3 additional information selective removal of copper with chelating agents, e.g. EDTA or N,N-diethyldithiocarbamate produces an inactive enzyme, CN- treatment gives fully copper-depleted apoform, indication that copper affects the enzyme stability but not the enzyme conformation 439912 1.10.3.3 NaCl induces the ascorbate oxidase activity 724853