Olsen J, Davis L
Biochim Biophys Acta. 1976 Sep 14;445(2):324-9. doi: 10.1016/0005-2744(76)90086-3.
Horseradish peroxidase (1.11.1.7), lactoperoxidase (1.11.1.7), and the fragment of cytochrome c known as microperoxidase have been shown to catalyze the oxidation of reduced dithiothreitol in an oxygen-consuming reaction. Evidence for horseradish peroxidase intermediates compound III and compound II has been observed, although ferroperoxidase was not identified during the course of the reaction. The stoichiometry has been extablished as 1 : 1 for oxygen consumed to dithiothreitol oxidized. Cysteine and glutathione have also been shown to be substrates for horseradish peroxidase oxidase reaction.
辣根过氧化物酶(1.11.1.7)、乳过氧化物酶(1.11.1.7)以及细胞色素c的片段即微过氧化物酶,已被证明可在耗氧反应中催化还原型二硫苏糖醇的氧化。已观察到辣根过氧化物酶中间体化合物III和化合物II的相关证据,尽管在反应过程中未鉴定出亚铁过氧化物酶。已确定耗氧量与氧化的二硫苏糖醇的化学计量比为1:1。半胱氨酸和谷胱甘肽也已被证明是辣根过氧化物酶氧化反应的底物。