کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1939959 | 1050771 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Oxidative modification of quercetin by hemeproteins Oxidative modification of quercetin by hemeproteins](/preview/png/1939959.png)
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 b5. 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.
Journal: Biochemical and Biophysical Research Communications - Volume 342, Issue 2, 7 April 2006, Pages 459–464