Decarboxylation of 3,4-Dihydroxyphenylalanine (DOPA) by Erythrocytes: A Reaction Promoted by Methemoglobin and Other Ferriheme Proteins

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Abstract
The decarboxylation of DOPA by erythrocyte hemolysates differs from DOPA decarboxylation catalyzed by aromatic aminoacid decarboxylases that contain vitamin B(6) in several significant respects. The ability of erythrocyte hemolysates to decarboxylate DOPA is associated with interaction between DOPA and methemoglobin; the ferriheme protein is reduced and DOPA is decarboxylated, probably after oxidation to a quinone intermediate. An analogous reaction takes place between DOPA and other ferriheme proteins, such as metmyoglobin and cytochrome c. This phenomenon may be of significance in relation to the side effects observed in patients with Parkinson's disease who are treated with very large doses of DOPA.