論文

査読有り
2013年6月

Interaction between NADH and electron-transferring flavoprotein from Megasphaera elsdenii

JOURNAL OF BIOCHEMISTRY
  • Kyosuke Sato
  • ,
  • Yasuzo Nishina
  • ,
  • Kiyoshi Shiga

153
6
開始ページ
565
終了ページ
572
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/jb/mvt026
出版者・発行元
OXFORD UNIV PRESS

Electron-transferring flavoprotein (ETF) from the anaerobic bacterium Megasphaera elsdenii is a heterodimer containing two FAD cofactors. Isolated ETF contains only one FAD molecule, FAD-1, because the other, FAD-2, is lost during purification. FAD-2 is recovered by adding FAD to the isolated ETF. The two FAD molecules in holoETF were characterized using NADH. Spectrophotometric titration of isolated ETF with NADH showed a two-electron reduction of FAD-1 according to a monophasic profile indicating that FAD-1 receives electrons from NADH without involvement of FAD-2. When holoETF was titrated with NADH, FAD-2 was reduced to an anionic semiquinone and then was fully reduced before the reduction of FAD-1. The midpoint potential values at pH 7 were +81, -136 and -279 mV for the reduction of oxidized FAD-2 to semiquinone, semiquinone to the fully reduced FAD-2 and the two-electron reduction of FAD-1, respectively. Both FAD-1 and FAD-2 in holoETF were reduced by excess NADH very rapidly. The reduction of FAD-2 was slowed by replacement of FAD-1 with 8-cyano-FAD indicating that FAD-2 receives electrons from FAD-1 but not from NADH directly. The present results suggest that FAD-2 is the counterpart of the FAD in human ETF, which contains one FAD and one AMP.

Web of Science ® 被引用回数 : 14

リンク情報
DOI
https://doi.org/10.1093/jb/mvt026
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000319751700009&DestApp=WOS_CPL

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