このエントリーをはてなブックマークに追加
ID 39968
本文ファイル
著者
Yamamoto, Sohei
Michibata, Hitoshi
キーワード
Transition metal
Disulfide bonds
Vanadium
Reductase
Ascidians
NDC
生物科学・一般生物学
抄録(英)
Ascidians (tunicates or sea squirts) accumulate extremely high levels of vanadium as the reduced form V(III) in extremely acidic vacuoles in their blood cells. Several key proteins related to vanadium accumulation have been isolated from vanadium-rich ascidians and their physiological functions characterized. Of these, vanabins are small, cysteine-rich proteins that have been identified only in vanadium-rich ascidians. Our previous study revealed that Vanabin2 can act as a V(V)-reductase. The current study examines the role of cysteine and several other amino acid residues of Vanabin2 in V(V)-reduction. When all eighteen cysteine residues of Vanabin2 were substituted with serine residues, the V(V)-reductase activity was lost. Substitutions of three, structurally clustered cysteines in three different regions resulted in a moderate decrease in reductase activity, suggesting that more than a single cysteine pair is responsible for the V(V)-reductase activity of Vanabin2. Mutations in the V(IV)-binding domains caused either an increase or decrease in activity but no mutation caused the complete loss of activity. These results suggest that some pairs, but more than a single pair, of cysteine residues are necessary for the V(V)-reductase activity of Vanabin2.
掲載誌名
Inorganica Chimica Acta
420巻
開始ページ
47
終了ページ
52
出版年月日
2014-08-24
出版者
Elsevier B.V.
ISSN
0020-1693
NCID
出版者DOI
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) 2013 Elsevier B.V. All rights reserved.
関連情報
This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
関連情報(IsVersionOf)
http:doi.org/10.1016/j.ica.2013.11.023
部局名
理学研究科