Molecular mechanism of the transport and reduction pathway of vanadium in ascidians

Coordination Chemistry Reviews Volume 255 Issue 19-20 Page 2249-2257 published_at 2011
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Title ( eng )
Molecular mechanism of the transport and reduction pathway of vanadium in ascidians
Creator
Michibata Hitoshi
Source Title
Coordination Chemistry Reviews
Volume 255
Issue 19-20
Start Page 2249
End Page 2257
Abstract
Metal ions are required for physiologically essential functions such as metalloenzymatic reactions, redox reactions, electron transfer, regulation of transcription factor activity, and respiration in living cells. Generally, metal ions are homeostatically maintained at very low concentrations in the sub-micromolar to micromolar range in living cells. However, some organisms, called hyperaccumulators, collect extremely high levels of metal ions, thereby providing experimental systems in which to study the mechanisms underlying the selective accumulation of metal ions. Typical of such organisms are the ascidians, more commonly known as sea squirts or tunicates. They are sessile marine animals belonging to the chordates. Several species of ascidians are known to accumulate extremely high levels of vanadium ions in their blood cells. Vanadium is usually in the V-V state in the natural environment, but in ascidians, most of vanadium is reduced to V-III via V-IV during the assimilation process. In this review, we first summarize the history of the studies on vanadium accumulation in ascidians and then focus on the recent progress of molecular studies, especially on the transport and reduction of vanadium, using primarily two ascidian species, Ascidia sydneiensis samea and Ciona intestinalis. Several candidate genes for V-IV transporters and enzymes catalyzing the redox reactions of V-V/V-IV are addressed in detail. The function of accumulated V-III is discussed in relation to redox reactions. (C) 2011 Elsevier B.V. All rights reserved.
Keywords
Vanadium
Sulfate
Proton
Ascidian
Redox
Membrane transporters
NDC
Biology [ 460 ]
Language
eng
Resource Type journal article
Publisher
Elsevier Science SA
Date of Issued 2011
Rights
(c) 2011 Elsevier B.V. All rights reserved.
Publish Type Author’s Original
Access Rights open access
Source Identifier
[ISSN] 0010-8545
[DOI] 10.1016/j.ccr.2011.01.012
[NCID] AA00619249
[DOI] http://dx.doi.org/10.1016/j.ccr.2011.01.012