Mazzini A, Dradi E, Favilla R, Fava A, Cavatorta P, Abdallah M A
Eur J Biochem. 1980 Feb;104(1):229-35. doi: 10.1111/j.1432-1033.1980.tb04420.x.
As previously reported [Favilla, R. & Cavatorta, P. (1975) FEBS Lett. 50, 324-329], the enzyme horse liver alcohol dehydrogenase catalyzes a reaction between NAD+ and H2O2. The final isolated product was then called NADX because of its unknown structure. In this paper the results of spectroscopic investigations on this compound are described. They indicate that only the nicotinamide moiety of the original NAD+ molecule was modified by the action of hydrogen peroxide. From the 1H and 13C nuclear magnetic resonance spectra of NADX the following structure was deduced: adenosine(5')diphospho(5)-beta-D-ribose-NH-CH = C(CHO)-CONH2. This structure is consistent with both ultraviolet and reactivity measurements performed on NADX. A tentative mechanism for the whole peroxidatic reaction pathway leading to NADX is finally proposed.
如先前报道[法维拉，R. & 卡瓦托塔，P.（1975年）《欧洲生物化学学会联合会快报》50，324 - 329]，马肝醇脱氢酶催化NAD⁺与H₂O₂之间的反应。由于其结构未知，最终分离出的产物被称为NADX。本文描述了对该化合物进行光谱研究的结果。结果表明，原始NAD⁺分子中只有烟酰胺部分被过氧化氢作用修饰。从NADX的¹H和¹³C核磁共振光谱推导出以下结构：腺苷(5')二磷酸(5)-β-D-核糖-NH-CH = C(CHO)-CONH₂。该结构与对NADX进行的紫外和反应性测量结果均一致。最后提出了导致NADX的整个过氧化物酶反应途径的初步机制。
