Metal Ion Selectivity of the Vanadium(V)-Reductase Vanabin2
Dalton Transactions Volume 42
Page 11921-11925
published_at 2013
アクセス数 : 722 件
ダウンロード数 : 194 件
今月のアクセス数 : 0 件
今月のダウンロード数 : 0 件
この文献の参照には次のURLをご利用ください : https://ir.lib.hiroshima-u.ac.jp/00039965
| File | |
| Title ( eng ) |
Metal Ion Selectivity of the Vanadium(V)-Reductase Vanabin2
|
| Creator |
Kitayama Hiroki
Yamamoto Sohei
Michibata Hitoshi
|
| Source Title |
Dalton Transactions
|
| Volume | 42 |
| Start Page | 11921 |
| End Page | 11925 |
| Abstract |
In a previous study, Vanabin2, a member of a family of V(IV)-binding proteins, or Vanabins, was shown to act as a V(V)-reductase. The current study assesses the ability of Vanabin2 to reduce various transition metal ions in vitro. An NADPH-coupled oxidation assay yielded no evidence of reduction activity with the hexavalent transition metal anions, MoVIO42- and WVIO42-, or with three divalent cations, Mn(II), Ni(II), and Co(II). Although Cu(II) is readily reduced by glutathione and is gradually oxidized in air, this process was not affected by the presence of Vanabin2. In the experiments conducted thus far, Vanabin2 acts only as a V(V)-reductase. This high selectivity may account for the metal ion selectivity of vanadium accumulation in ascidians.
|
| NDC |
Biology [ 460 ]
|
| Language |
eng
|
| Resource Type | journal article |
| Publisher |
Royal Society of Chemistry
|
| Date of Issued | 2013 |
| Rights |
Copyright (c) The Royal Society of Chemistry 2013
|
| Publish Type | Author’s Original |
| Access Rights | open access |
| Source Identifier |
[ISSN] 1477-9226
[NCID] AA11810256
[DOI] 10.1039/c3dt50404b
[DOI] http://doi.org/10.1039/c3dt50404b
isVersionOf
|
