論文

査読有り
2013年7月

Decomposition of the fluorescence spectra of two FAD molecules in electron-transferring flavoprotein from Megasphaera elsdenii

Journal of Biochemistry
  • Kyosuke Sato
  • ,
  • Yasuzo Nishina
  • ,
  • Kiyoshi Shiga

154
1
開始ページ
61
終了ページ
66
記述言語
英語
掲載種別
DOI
10.1093/jb/mvt027

Electron-transferring flavoprotein (ETF) from Megasphaera elsdenii contains two FAD molecules, FAD-1 and FAD-2. FAD-2 shows an unusual absorption spectrum with a 400-nm peak. In contrast, ETFs from other sources such as pig contain one FAD and one AMP with the FAD showing a typical flavin absorption spectrum with 380-and 440-nm peaks. It is presumed that FAD-2 is the counterpart of the FAD in other ETFs. In this study, the FAD-1 and FAD-2 fluorescence spectra were determined by titration of FAD-1-bound ETF with FAD using excitation-emission matrix (EEM) fluorescence spectroscopy. The EEM data were globally analysed, and the FAD fluorescence spectra were calculated from the principal components using their respective absorption spectra. The FAD-2 fluorescence spectrum was different from that of pig ETF, which is more intense and blue-shifted. AMP-free pig ETF in acidic solution, which has a comparable absorption spectrum to FAD-2, also had a similar fluorescence spectrum. This result suggests that FAD-2 in M. elsdenii ETF and the FAD in acidic AMP-free pig ETF share a common microenvironment. A review of published ETF fluorescence spectra led to the speculation that the majority of ETF molecules in solution are in the conformation depicted by the crystal structure. © 2013 The Authors 2013. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

リンク情報
DOI
https://doi.org/10.1093/jb/mvt027
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/23606284

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