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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-2-18
pubmed:abstractText
Experimental evidence documenting the formation of a relatively stable V(IV) species appears to be important with regard to the biochemical mechanism of reduction of vanadate by enzymatic systems. The present study demonstrates that a mixture of vanadate and glutathione reductase/nicotinamide-adenine-dinucleotide phosphate (NADPH), in phosphate (pH 7.2) buffer generates V(IV) under ambient conditions. Once formed, V(IV) does not rapidly autoxidize so as to defy detection by electron spin resonance (ESR) spectroscopy. The aerobic environment was guaranteed by preparing reaction mixtures in well stirred, wide mouth, standard test tubes in air over a period of 50 minutes, and by making ESR measurements in nuclear magnetic resonance (NMR) sample tubes as well as oxygen-permeable Teflon tubes. The V(IV) ESR signal intensity was found to increase linearly with time elapsed after reaction initiation. The linear growth of the V(IV) species also shows that this species is fairly stable, over a period of at least 50 minutes. Similar V(IV) stability data were obtained from VOSO4, a model compound as a source of V(IV). The results obtained in the present study demonstrated that V(IV) can be generated in the reduction of V(IV) by glutathione reductase in the presence of NADPH under aerobic condition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0091-7370
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
422-7
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:articleTitle
Vanadium (IV) formation in the reduction of vanadate by glutathione reductase/NADPH and the role of molecular oxygen.
pubmed:affiliation
Pathology and Physiology Research Branch, National Institute for Occupational Safety and Health, Morgantown, WV 26505, USA.
pubmed:publicationType
Journal Article