Methaemoglobin-catalysed formation of dopa and 6-OH-dopa from tyrosine

An extract of bovine retina and choroid with tyrosine hydroxylating and dopa-oxidizing capacity also showed marked formation of 6-OH-dopa on incubation with tyrosine and ascorbic acid. The extract contained appreciable amounts of methaemoglobin as determined spectrophotometrically, and boiled extracts also showed catalytic activity. The effect of methaemoglobin on the oxidation of tyrosine and dopa was therefore investigated. Methaemoglobin catalysed the formation of dopa and 6-OH-dopa in the presence of tyrosine and ascorbic acid. Hydrogen peroxide plays an important role in this reaction: the rates of formation of both dopa and 6-OH-dopa were increased by addition of hydrogen peroxide but diminished by addition of catalase. Methaemoglobin also catalysed the formation of cysteinyldopa from dopa and cysteine.