Houée-Levin C, Gardès-Albert M, Benzineb K, Rouscilles A, Ferradini C
Laboratoire de Chimie Physique, Université Paris V, France.
Free Radic Res Commun. 1990;11(1-3):127-36. doi: 10.3109/10715769009109675.
The one-electron reduction of daunorubicin, an anthracycline antibiotic, intercalated in DNA or in the apoprotein of the riboflavin binding protein, was studied by gamma radiolysis. The two reduction mechanisms appear very similar to the one found for the non-intercalated drug. Hydrogen peroxide, which oxidizes non-intercalated hydroquinone daunorubicin with two electrons in one step (C. Houée-Levin, M. Gardès-Albert and C. Ferradin, FEBS lett., 173, 27-30, (1984], reacts with daunorubicin hydroquinone in DNA but not in the protein. It appears thus that the site accessibility to hydrogen peroxide in DNA is better than in the protein. Biological consequences are discussed.
通过γ射线辐解研究了嵌入DNA或核黄素结合蛋白脱辅基蛋白中的蒽环类抗生素柔红霉素的单电子还原。这两种还原机制似乎与未嵌入的药物的还原机制非常相似。过氧化氢能一步将未嵌入的对苯二酚柔红霉素氧化，转移两个电子（C. 胡埃 - 莱万、M. 加尔德斯 - 阿尔贝和C. 费拉丹，《欧洲生物化学学会联合会快报》，173，27 - 30，（1984年）），它能与DNA中的柔红霉素对苯二酚反应，但不能与蛋白质中的反应。因此，DNA中过氧化氢的可及位点似乎比蛋白质中的更好。文中讨论了其生物学后果。
