The Type-2 copper ion in bovine serum amine oxidase (BSAO) was first replaced by cobalt(II) ion. The enzymatic activity of Co(II)BSAO was 13.3% of that of native BSAO. The various spectral data indicated that the Co(II) center has tetrahedral geometry (high-spin state) and is linked by two nitrogens and two oxygens. It was also found that the putative organic chromophore suggested by many investigators exhibits a positive CD band near 370 nm and a negative CD band near 440 nm.
The structure of copper binding site in bovine serum amine oxidase (BSAO) treated with diethyldithiocarbamate ion(DDC) was discussed by comparing its absorption and electron spin resonance spectra with those of a model copper complex. The structure of the model complex, [Cu(2,2′-bipyridine)(DDC)]+, suggested that at least two nitrogen atoms are coordinated around the copper ion in the native BSAO. Some organic chromophore from which the pink color of BSAO stems was also observed as the difference of the absorption spectra in the region of 450 to 600 nm between BSAO-DDC and the model complex.
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