aromatic ring (with hetero atoms other than nitrogen atoms)
HIS 106(Copper-3a);HIS 62;HIS 104(Copper-3b);HIS 60(Copper-2)
HIS 445;CYS 507;HIS 512;MET 517(Copper-1);HIS 450;HIS 506(Copper-3a);HIS 508(Copper-3b);HIS 448(Copper-2)
Preliminary crystallographic study of ascorbic acid oxidase from green zucchini squash.
A new crystalline modification of the copper enzyme ascorbate oxidase.
Preliminary X-ray crystal structure and partial cDNA-sequence of ascorbate oxidase from zucchini.
X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.
The role of copper in the stability of ascorbate oxidase towards denaturing agents.
X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini.
Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms.
EPR spectra of type 3 copper centers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase.
Inhibition of ascorbate oxidase by phenolic compounds. Enzymatic and spectroscopic studies.
Role of quaternary structure in the stability of dimeric proteins: the case of ascorbate oxidase.
Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements.
The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase.
Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time.
Azide binding to the trinuclear copper center in laccase and ascorbate oxidase.
Protein packing: dependence on protein size, secondary structure and amino acid composition.
Upward shift of the pH optimum of Acremonium ascorbate oxidase.
Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies.
Coppers can be classified into three types (see literature [7], [8] & laccase;T00215 in EzCatDB): Type I copper (blue copper); Copper-1 in this enzyme Type II copper (non-blue copper); Copper-2 Type III copper (EPR-non-detectable copper); Copper-3a & copper-3b in this enzyme. The copper-2, -3a and -3b form a trinuclear copper site, to which an oxygen is bound, whereas the cooper-1 is a monocuclear copper site, to which an organic substrate is bound (see laccase;T00215). This enzyme catalyzes the following reactions: (A) Oxidation (dehydrogenation) of organic substrate at mononuclear coper site: (B) Electron transfer from mononuclear copper site to trinuclear copper site: (C) O2 reduction to produce H2O at trinuclear copper site: