Protein oxidation by the cytochrome P450 mixed-function oxidation system.
Protein oxidation by the cytochrome P450 mixed-function oxidation system.
复制标题
细胞色素 P450 混合功能氧化系统对蛋白质进行氧化。
DOI:
10.1016/j.bbrc.2005.07.203
复制
发表时间:
2005
影响因子:
3.1
通讯作者:
Berlett,BarbaraS
中科院分区:
文献类型:
--
作者:
Stadtman,EarlR;Arai,Hirofumi;Berlett,BarbaraS
This mini-review summarizes results of studies on the oxidation of proteins and low-density lipoprotein (LDL) by various mixed-function oxidation (MFO) systems. Oxidation of LDL by the O2/FeCl3/H2O2/ascorbate MFO system is dependent on all four components and is much greater when reactions are carried out in the presence of a physiological bicarbonate/CO2buffer system as compared to phosphate buffer. However, FeCl3in this system could be replaced by hemin or the heme-containing protein, hemoglobin, or cytochrome c. Oxidation of LDL by the O2/cytochrome P450 cytochrome c reductase/NADPH/FeCl3MFO system is only slightly higher (25%) in the bicarbonate/CO2buffer as compared to phosphate buffer, but is dependent on all components except FeCl3. Omission of FeCl3led to a 60% loss of activity. These results suggest that peroxymonobicarbonate and/or free radical derivatives of bicarbonate ion and/or CO2might contribute to LDL oxidation by these MFO systems.