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Characterization of vanadate-based transition-state-analogue complexes of phosphoglucomutase by spectral and NMR techniques

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00463a021· OSTI ID:6170455
Near ultraviolet spectral studies were conducted on two inhibitor complexes obtained by treating the dephospho form of the phosphoglucomutase{center dot}Mg{sup 2+} complex with inorganic vanadate in the presence of either glucose 1-phosphate or glucose 6-phosphate. Part of the spectral differences between the two inhibitor complexes arises because the glucose phosphate moiety in the complex derived from glucose 1-phosphate binds to the enzyme in a different way from the glucose phosphate moiety in the complex derived from glucose 6-phosphate and because these alternative binding modes produce different environmental effects on the aromatic chromophores of the dephospho enzyme. These spectra differences are strikingly similar to those induced by the binding of glucose 1-phosphate and glucose 6-phosphate to the phospho enzyme. {sup 31}P NMR studies of the phosphate group in these complexes also provide support for this binding pattern. Difference spectroscopy was used to resolve the spectrum of both inhibitor complexes to obtain the absorbance of their oxyvanadium chromophores. A spectrum more nearly like that of a normal vanadate ester is observed for the oxyvanadium chromophore in the corresponding complex involving glucose 1-phosphate and Li{sup +} instead of Mg{sup 2+}.
OSTI ID:
6170455
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:11; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English