El Behery Mohammed, Fujimura Mika, Kimura Tetsunari, Tsubaki Motonari
Department of Chemistry, Graduate School of Science, Kobe University, Nada-ku, Kobe, Hyogo, 657-8501, Japan.
Biochem Biophys Rep. 2020 Jan 17;21:100730. doi: 10.1016/j.bbrep.2020.100730. eCollection 2020 Mar.
We studied human 101F6 protein to clarify its physiological function as a ferric reductase and its relationship to tumor suppression activity. We found for the first time that purified 101F6 both in detergent micelle state and in phospholipid bilayer nanodisc state has an authentic ferric reductase activity by single turnover kinetic analyses. The kinetic analysis on the ferrous heme oxidation of reduced 101F6 upon the addition of a ferric substrate, ferric ammonium citrate (FAC), showed concentration-dependent accelerations of its reaction with reasonable values of and . We further verified the authenticity of the ferric reductase activity of 101F6 using nitroso-PSAP as a Fe-specific colorimetric chelator. 101F6 in nanodisc state showed higher efficiency for FAC than in detergent micelle state.
我们研究了人类101F6蛋白，以阐明其作为铁还原酶的生理功能及其与肿瘤抑制活性的关系。我们首次通过单周转动力学分析发现，处于去污剂胶束状态和磷脂双层纳米盘状态的纯化101F6均具有真正的铁还原酶活性。在添加铁底物柠檬酸铁铵（FAC）后，对还原型101F6的亚铁血红素氧化进行的动力学分析表明，其反应呈浓度依赖性加速，具有合理的 值和 值。我们进一步使用亚硝基-PSAP作为铁特异性比色螯合剂验证了101F6铁还原酶活性的真实性。纳米盘状态的101F6对FAC的效率高于去污剂胶束状态。
