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. 1978 Nov;75(11):5395–5399. doi: 10.1073/pnas.75.11.5395

Photodestruction of pheomelanin: role of oxygen.

M R Chedekel, S K Smith, P W Post, A Pokora, D L Vessell
PMCID: PMC392970  PMID: 281688

Abstract

Pheomelanin, the red-brown polymeric pigment in the skin and hair of red-headed humans, is composed of a protein fraction covalently bound to a colored chromophore. Photolysis of aerated aqueous phemelanin solutions, isolated from human red hair, results in destruction of the chromophore and liberation of the peptide fraction. The rate of photolysis depends on the pH and the concentration of both pigment and oxygen and is slightly inhibited by the enzyme superoxide dismutase (superoxide:superoxide oxidoreductase EC 1.15.1.1). Pheomelanin photolyzed in the presence of nitroblue tetrazolium results in the formation of a blue diformazan, whether or not oxygen is present. Superoxide dismutase inhibits the aerobic photoreduction of nitroblue tetrazolium whereas, in the absence of oxygen, no inhibition is observed. These experiments strongly suggest the involvement of superoxide in the aerobic photolysis of pheomelanin and point out a possible mechanism for ultraviolet-induced cell damage in redheads.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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