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Vanadium(V) complexes with 3-phosphoglycerate and other. cap alpha. -hydroxy acids: interactions with phosphoglycerate mutase

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5332940

/sup 51/V nuclear magnetic resonance (NMR) studies of vanadate in aqueous solution have shown that inorganic vanadate does not bind strongly to rabbit muscle phosphoglycerate mutase. However, in the presence of 3-phosphoglycerate, strong binding to this enzyme does occur, as indicated by a large decrease in intensity of the NMR signal. These observations support the hypothesis that the strong inhibition of phosphoglycerate mutase by vanadate (K/sub i/ approx. = 1 ..mu..M) is caused by a species such as 2-vanado-3-phosphoglycerate which binds to the dephosphorylated enzyme as a transition state analogue. In the absence of enzyme but in the presence of either 3-phosphoglycerate or lactate, the vanadium NMR spectrum shows a variety of resonances, one of which can be attributed to ester formation at the ..cap alpha..-hydroxy group to yield a tetrahedrally coordinated vanadate ester. Other resonances are attributed to the formation in solution of various 5- and 6-coordinated complexes of differing stoichiometry and charge which have been characterized on the basis of vanadate concentration, ligand concentration and pH studies. Equilibrium constants for formation of the various vanadate derivatives have been determined. The formation of the vanadate/3-phosphoglycerate/phosphoglycerate mutase complex has been examined in detail and an equilibrium constant for formation determined.

Research Organization:
Simon Fraser Univ., Burnaby, British Columbia
OSTI ID:
5332940
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:6; ISSN FEPRA
Country of Publication:
United States
Language:
English