Abstract

Publisher Summary An enzyme-catalyzed reaction may display a very broad range of values for kinetic isotope effects, depending on reaction conditions. Because the methods of determination and ways of thinking about isotope effects originate with chemical reactions, the variation of values has led to considerable conceptual difficulty, poorly designed experiments, and faulty interpretation of results. Thus, this chapter defines the variety of hydrogen isotope effects within a logical and practical framework, and outlines appropriate experimental designs for the determination of each. It is reported that the primary limitation encountered in the use of isotope effects in enzymology is the need for extreme precision. Unlike steady-state kinetics, which are concerned with parameter estimations, isotope effects are defined as ratios of parameters that, in addition, have quantitative significance only as diminished ratios to yet another isotope effect.

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