Hartzell P L, Zvilius G, Escalante-Semerena J C, Donnelly M I
Biochem Biophys Res Commun. 1985 Dec 31;133(3):884-90. doi: 10.1016/0006-291x(85)91218-5.
To identify the electron acceptor of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum, we have purified the enzyme to homogeneity. The purified enzyme is absolutely dependent on coenzyme F420 (a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative) for activity. Several alternative electron acceptors are ineffectual in the reaction. Changes in the absorption spectra of reaction mixtures indicate that 1.1 mol of coenzyme F420 is reduced per mol of substrate oxidized. The reaction is reversible and the equilibrium favors oxidation of methylenetetrahydromethanopterin.
为了鉴定嗜热自养甲烷杆菌亚甲基四氢甲蝶呤脱氢酶的电子受体，我们已将该酶纯化至同质。纯化后的酶活性绝对依赖于辅酶F420（一种7,8-二去甲基-8-羟基-5-去氮核黄素衍生物）。几种替代电子受体在该反应中无效。反应混合物吸收光谱的变化表明，每氧化1摩尔底物，有1.1摩尔辅酶F420被还原。该反应是可逆的，且平衡有利于亚甲基四氢甲蝶呤的氧化。
