Prabhakaran K, Harris E B
Experientia. 1985 Dec 15;41(12):1571-2. doi: 10.1007/BF01964812.
Among mycobacteria, Mycobacterium leprae is unique in its ability to oxidize a variety of diphenols to quinones in vitro. What physiologic role o-diphenoloxidase has in the organism remained unknown. Reducing substrates like NADPH, NADH and ascorbic acid reacted with the quinone formed from dopa (3,4-dihydroxyphenylalanine); the substrates were oxidized and the quinone was reduced back to diphenol in the process. Since the quinone undergoes reversible oxidation-reduction, diphenoloxidase might serve as an alternative respiratory mechanism in M. leprae for the utilization of other substrates, as has been reported in plants.
在分枝杆菌中，麻风分枝杆菌在体外将多种二酚氧化为醌的能力是独特的。邻二酚氧化酶在该生物体中具有何种生理作用尚不清楚。像NADPH、NADH和抗坏血酸这样的还原性底物与由多巴（3,4-二羟基苯丙氨酸）形成的醌发生反应；底物被氧化，在此过程中醌被还原回二酚。由于醌经历可逆的氧化还原反应，邻二酚氧化酶可能作为麻风分枝杆菌利用其他底物的一种替代呼吸机制，正如在植物中所报道的那样。
