Abstract
Reactions catalysed by enzymes usually involve the successive formation of several intermediate compounds (enzyme–substrate complexes, covalent intermediates, conformers of the enzyme or the substrate). Kinetic methods have provided a fertile approach to the investigation of such labile intermediates. The Review summarises the kinetic laws of catalytic reactions involving labile intermediates in prestationary and stationary states. The relaxation kinetics of a multistage catalytic reaction is also examined.
The investigation of labile intermediate compounds is inseparably connected with the development of methods of "fast" kinetics. The Review therefore discusses "flow", "flash", and "temperature jump" methods and the possibility of applying them to enzymic reactions. Rather more detailed consideration is given to the formal kinetics of the appearance of intermediate compounds in reactions of the most thoroughly studied enzymes – catalase, α-chymotrypsin, peroxidase, ribonuclease, and aspartate aminotransferase.
A list of 236 references is included.