Abstract
Steady-state kinetics can provide information about the overall reaction pathway for multiple substrate reactions, the specificity of the enzyme for specific substrate structures, and lower bounds for the specific rate constants in a mechanism. However, the kinetic parameters measured are complex functions of the specific rate constants, so that individual rate constants rarely can be determined and little information is obtained about mechanistic intermediates. To elucidate the details of an enzymatic mechanism and to measure rate constants for elementary steps, kinetic experiments must be carried out at high enzyme concentrations where enzyme-substrate species are significantly populated and can be directly detected. Because enzymes are very efficient catalysts, fast reaction techniques are often needed to study the transient kinetics. This chapter is discusses transient kinetic studies to biochemists. First, the theoretical bases, for analyzing the rate equations, associated with typical mechanisms, are discussed in the chapter. Second, a brief description of the various types of stopped-flow, rapid quench, and temperature jump equipment is given. Finally, some examples of transient kinetic studies are described in the chapter.
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