期刊
INORGANIC CHEMISTRY
卷 49, 期 9, 页码 4245-4256出版社
AMER CHEMICAL SOC
DOI: 10.1021/ic100080k
关键词
-
资金
- General Medical Institute at the National Institutes of Health [GM40525]
Although dogma states that vanadate is readily reduced by glutathione, cysteine, and other thiols, there are several examples documenting that vanadium(V)-sulfur complexes can form and be observed. This conundrum has impacted life scientists for more than two decades Investigation of this problem requires an understanding of both the complexes that form from vanadium(IV) and (V) and a representative thiol in aqueous solution The reactions of vanadate and hydrated vanadyl cation with 2-mercaptoethanol have been investigated using multinuclear NMR, electron paramagnetic resonance (EPA), and UV-vis spectroscopy Vanadate forms a stable complex of 2.2 stoichiometry with 2-mercaptoethanol at neutral and alkaline pH. In contrast, vanadate can oxidize 2-mercaptoethanol; this process is favored at low pH and high solute concentrations The complex that forms between aqueous vanadium(IV) and 2-mercaptoethanol has a 1 2 stoichiometry and can be observed at high pH and high 2-mercaptoethanol concentration The solution structures have been deduced based on coordination induced chemical shifts and speciation diagrams prepared This work demonstrates that both vanadium(IV) and (V)-thiol complexes form and that redox chemistry also takes place Whether reduction of vanadate takes place is governed by a combination of parameters. pH, solute- and vanadate-concentrations and the presence of other complexing ligands On the basis of these results it is now possible to understand the distribution of vanadium in oxidation states (IV) and (V) in the presence of glutathione, cysteine, and other thiols and begin to evaluate the forms of the vanadium compounds that exert a particular biological effect including the insulin-enhancing agents, antiamoebic agents, and interactions with vanadium binding proteins
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