血红素蛋白对槲皮素的氧化修饰。
Oxidative modification of quercetin by hemeproteins.
作者信息
Cherviakovsky Egor M, Bolibrukh Dmitry A, Baranovsky Alexander V, Vlasova Tamara M, Kurchenko Vladimir P, Gilep Andrey A, Usanov Sergey A
机构信息
Institute of Bioorganic Chemistry, Academy of Sciences of Belarus, Kuprevicha st., 5/2, Minsk 220141, Belarus.
出版信息
Biochem Biophys Res Commun. 2006 Apr 7;342(2):459-64. doi: 10.1016/j.bbrc.2006.02.001. Epub 2006 Feb 9.
The ability of a number of hemeproteins to oxidize the flavonoid quercetin has been shown. It was found that quercetin undergoes chemical modification in the presence of cytochrome c, myoglobin, and hemoglobin but not cytochrome b(5). In the range of investigated proteins the most effective oxidant appears to be cytochrome c. Chromatographic analysis of the reaction mixture revealed a number of quercetin oxidation products. The main oxidation product was purified and characterized by means of LC-MS and NMR analyses. It has a dimeric structure similar to the product of quercetin oxidation by horseradish peroxidase and is formed during radical-driven reactions. Our results indicate that a number of hemeproteins can react and modify biologically active flavonoids. However, these reactions might also lead to the generation of active species with deleterious consequences for the cellular macromolecules.
已证明多种血红素蛋白具有氧化类黄酮槲皮素的能力。研究发现，槲皮素在细胞色素c、肌红蛋白和血红蛋白存在的情况下会发生化学修饰，但在细胞色素b(5)存在时不会。在所研究的蛋白质范围内，最有效的氧化剂似乎是细胞色素c。对反应混合物进行色谱分析，发现了多种槲皮素氧化产物。通过液相色谱-质谱联用（LC-MS）和核磁共振（NMR）分析对主要氧化产物进行了纯化和表征。它具有与辣根过氧化物酶氧化槲皮素的产物相似的二聚体结构，并且是在自由基驱动的反应过程中形成的。我们的结果表明，多种血红素蛋白可以与生物活性类黄酮发生反应并对其进行修饰。然而，这些反应也可能导致活性物质的产生，对细胞大分子产生有害影响。
Zotero 插件