Decarboxylation of 3,4-dihydroxyphenylalanine (DOPA) by erythrocytes: a reaction promoted by methemoglobin and other ferriheme proteins. Academic Article uri icon

Overview

MeSH Major

  • Cytochromes
  • Dihydroxyphenylalanine
  • Erythrocytes
  • Methemoglobin
  • Myoglobin
  • Peroxidases

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.

publication date

  • September 1972

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC426975

PubMed ID

  • 4403564

Additional Document Info

start page

  • 2505

end page

  • 8

volume

  • 69

number

  • 9