The use of 17O-NMR in the study of bond cleavage during the hydrolysis of sulphate esters.
The use of 17O-NMR to investigate bond cleavage during the hydrolysis of sulphate esters in water enriched in 17O is described. Despite the inherent disadvantages of 17O for NMR studies, this work shows that, in favourable cases, 17O-NMR of 17O-enriched species is a powerful and sensitive tool for mechanistic studies. It is particularly useful when O-S cleavage occurs, resulting in the formation of S17O16O3(2-) (5% 17O), which can easily be detected at the biologically relevant mumole level. The method complements those using H2(18)O and has the advantage that in principle 17O can be detected in either of the hydrolysis products with little or no purification. It has been shown that sulphatase A (aryl-sulphate sulphohydrolase, EC 3.1.6.1) cleaves the O-S bond while functioning as a cerebroside sulphatase, as it does when functioning as an aryl- or glycosulphatase.
D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010103:Oxygen Isotopes; D013429:Sulfatases / Q000378:metabolism*
D010103:Oxygen Isotopes; D013429:Sulfatases