Wrona M Z, Dryhurst G
Department of Chemistry and Biochemistry, University of Oklahoma, Norman 73019.
Biochem Pharmacol. 1991 Apr 15;41(8):1145-62. doi: 10.1016/0006-2952(91)90653-m.
Peroxidase (EC 1.11.1.7)/H2O2, ceruloplasmin (human type X)/O2, and tyrosinase (EC 1.14.18.1)/O2 all oxidized the indolic neurotransmitter 5-hydroxytryptamine (5-HT) in the physiological pH domain. Peroxidase/H2O2 oxidized 5-HT at pH values down to about 2.5. All oxidation reactions generated complex mixtures of products which included at least one known neurotoxin, tryptamine-4,5-dione. In general, the enzymatic oxidation pathways paralleled the in vitro electrochemical oxidation of 5-HT which has permitted suggestions to be made concerning the probable mechanisms of the enzyme-mediated reactions.
过氧化物酶（EC 1.11.1.7）/过氧化氢、铜蓝蛋白（人类X型）/氧气和酪氨酸酶（EC 1.14.18.1）/氧气在生理pH范围内均能氧化吲哚类神经递质5-羟色胺（5-HT）。过氧化物酶/过氧化氢在pH值低至约2.5时就能氧化5-HT。所有氧化反应均产生复杂的产物混合物，其中包括至少一种已知的神经毒素色胺-4,5-二酮。一般来说，酶促氧化途径与5-HT的体外电化学氧化相似，这使得人们能够对酶介导反应的可能机制提出一些建议。
