論文

査読有り 国際誌
2020年3月

Direct measurements of ferric reductase activity of human 101F6 and its enhancement upon reconstitution into phospholipid bilayer nanodisc.

Biochemistry and biophysics reports
  • Mohammed El Behery
  • ,
  • Mika Fujimura
  • ,
  • Tetsunari Kimura
  • ,
  • Motonari Tsubaki

21
開始ページ
100730
終了ページ
100730
記述言語
英語
掲載種別
DOI
10.1016/j.bbrep.2020.100730

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 KM and Vmax. We further verified the authenticity of the ferric reductase activity of 101F6 using nitroso-PSAP as a Fe2+-specific colorimetric chelator. 101F6 in nanodisc state showed higher efficiency for FAC than in detergent micelle state.

リンク情報
DOI
https://doi.org/10.1016/j.bbrep.2020.100730
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32055716
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7005374