Abstract
The activity of aconitase has been compared in H 2O and in 99% D 2O, with deuteriocitrate and deuterioisocitrate as well as the protiated substrates, citrate, isocitrate, and aconitate. The rates of all six interconversions were markedly inhibited by D 2O; the conversion of aconitate to citrate was affected much more than the conversion of aconitate to isocitrate. The values obtained for Michaelis constants and maximum velocities satisfactorily predict equilibrium conditions in H 2O and D 2O. Negligible isotope effects were observed with deuteriocitrate or deuterioisocitrate; this observation is consistent with the hypothesis that the first (and rate-limiting) step in the dehydration of these compounds is the rupture of the CO rather than the CH bond.
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