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ID 26921
本文ファイル
著者
Kawakami, Norifumi
Amata, Yusuke
Kanamori, Kan
Gekko, Kunihiko
Michibata, Hitoshi
キーワード
Ascidian
Vanadium
Vanabin2
Redox
Thiol-disulfide exchange reaction
NDC
生物科学・一般生物学
抄録(英)
The unusual ascidian ability to accumulate high levels of vanadium ions at concentrations of up to 350 mM, a 107-fold increase over that found in seawater, has been attracting interdisciplinary attention for a century. Accumulated VV is finally reduced to VIII via VIV in ascidian vanadocytes. Reducing agents must therefore participate in the reduction. Previously, we identified a vanadium-binding protein, Vanabin2, in which all 18 cysteines form nine disulfide bonds. Here, we report that Vanabin2 is a novel vanadium reductase because partial cleavage of its disulfide bonds results in the reduction of VV to VIV. We propose that Vanabin2 forms a possible electron transfer cascade from the electron donor, NADPH, via glutathione reductase, glutathione, and Vanabin2 to the acceptor, and vanadium ions conjugated through thiol-disulfide exchange reactions.
掲載誌名
Biochimica et Biophysica Acta. Proteins and Proteomics
1794巻
4号
開始ページ
674
終了ページ
679
出版年月日
2009-04
出版者
Elsevier B.V.
ISSN
1570-9639
NCID
出版者DOI
PubMedID
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
Copyright (c) 2009 Elsevier B.V.
関連情報URL(IsVersionOf)
http://dx.doi.org/10.1016/j.bbapap.2009.01.007
部局名
理学研究科