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An Electron Paramagnetic Resonance Study of 3,4-Dihydroxyphenylethylamine ß-Hydroxylase

From the ¹ From the Laboratory of General and Comparative Biochemistry, National Institute of Mental Health, National Institutes of Health, Bethesda, Maryland 20014

1. The role of the copper in highly purified bovine adrenal 3,4-dihydroxyphenylethylamine ß-hydroxylase (dopamine ß-hydroxylase) has been studied with the use of electron paramagnetic resonance techniques. The results confirm our previous findings. Most of the protein-bound Cu²⁺ is reduced by treatment of the enzyme with ascorbate; a large part of the Cu⁺ in the reduced enzyme is reoxidized during the hydroxylation of substrate. These results support a reduction-oxidation role for the protein-bound copper.

2. Fumarate, an activator of dopamine ß-hydroxylase, appears to favor the oxidation of Cu⁺ to Cu²⁺. This effect of fumarate is discussed in terms of the mechanism of action of dopamine ß-hydroxylase.

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