Oxidation of the indole nucleus of 5-hydroxytryptamine and formation of dimers in the presence of peroxidase and H2O2.
5-Hydroxytryptamine (5-HT) is rapidly oxidized in the presence of peroxidase and H2O2. The major reaction product was isolated by gel chromatography and analyzed by mass spectroscopy. It is a 5-HT dimer formed under abstraction of two protons, most likely by the reaction at the C(4) position of two phenoxyradicals of 5-HT. In the presence of 5-HT an increased H2O2-consumption and a dose dependent reduction of the formation of reactive oxygen metabolites during H2O2 degradation was observed. The pattern of 5-HT reaction products separated by TLC was dependent on the H2O2 concentrations used. In the presence of albumen, plasma or tissue homogenates, massive binding of the 5-HT oxidation products to proteins was observed.
Heuther
G
G
Neurochemische Forschungsgruppe der Psychiatrischen Klinik, University of Göttingen, Federal Republic of Germany.
Reimer
A
A
Schmidt
F
F
Schuff-Werner
P
P
Brudny
M M
MM
D000418:Albumins / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000378:metabolism; D002855:Chromatography, Thin Layer; D006735:Horseradish Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D007211:Indoles / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D008163:Luminescent Measurements; D013058:Mass Spectrometry; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D051381:Rats; D012701:Serotonin / Q000378:metabolism*
D000418:Albumins; D007211:Indoles; D011506:Proteins; D012701:Serotonin; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D010544:Peroxidases