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ID 39965
file
creator
Kitayama, Hiroki
Yamamoto, Sohei
Michibata, Hitoshi
NDC
Biology
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.
journal title
Dalton Transactions
volume
Volume 42
start page
11921
end page
11925
date of issued
2013
publisher
Royal Society of Chemistry
issn
1477-9226
ncid
publisher doi
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
author
rights
Copyright (c) The Royal Society of Chemistry 2013
relation is version of URL
http://doi.org/10.1039/c3dt50404b
department
Graduate School of Science



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