Preparation and Characterization of Cobalt(II)-Substituted Bovine Serum Amine Oxidase1

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Abstract
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.

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