Metal ion selectivity of the vanadium(v)-reductase Vanabin2
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2013/DT/C3DT50404B
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1. Valency of vanadium in the vanadocytes ofAscidia gemmata separated by density-gradient centrifugation
2. Isolation of highly acidic and vanadium-containing blood cells from among several types of blood cell from ascidiidae species by density-gradient centrifugation
3. Scanning X-ray Microscopy of Living and Freeze-Dried Blood Cells in Two Vanadium-Rich Ascidian Species, Phallusia mammillata and Ascidia sydneiensis samea
4. Subunit C of the Vacuolar-Type ATPase from the Vanadium-Rich Ascidian Ascidia sydneiensis samea Rescued the pH Sensitivity of Yeast vma5 Mutants
5. Chloride channel in vanadocytes of a vanadium-rich ascidian Ascidia sydneiensis samea
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1. The acidic amino acid-rich C-terminal domain of VanabinX enhances reductase activity, attaining 1.3- to 1.7-fold vanadium reduction;Biochemistry and Biophysics Reports;2022-12
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4. Vanadium;Reference Module in Chemistry, Molecular Sciences and Chemical Engineering;2016
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