Bovine adrenal medulla 3,4-dihydroxyphenylethylamine β-hydroxylase has been further characterized. The enzyme consists of four subunits, two pairs of which are linked by disulfide bridges and two pairs of which are held together by noncovalent bonds. Preliminary evidence suggests that these subunits are identical. The activation of this enzyme by anions has been studied. The binding of anions to a basic group adjacent to the ionizable group at the active site has been proposed to explain the mechanism of activation by these compounds. No evidence has been found for an anioninduced conformational change.
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Craine et al. (1973) studied this question.
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