Kinetic isotope effects (KIE) occur when the substitution of an atom in a molecule with one of its isotopes changes the reaction rate. KIE provides insight into the reaction mechanism, particularly which bonds are being made or broken during the rate-determining step. Isotopes influence reaction rates primarily due to differences in mass, which affect bond vibrations and zero-point energy (ZPE).
A primary KIE arises when a bond to the isotopically substituted atom is broken or formed in the rate-determining step.
A secondary KIE occurs when the isotopically substituted atom is not directly involved in bond-breaking or bond-forming in the rate-determining step but still influences the reaction.
Examples:
(a) SN1 Reaction of Tertiary Alkyl Halides
(b) E1 Elimination
An inverse KIE occurs when the heavier isotope reacts faster than the lighter isotope. This unusual effect arises due to differences in ZPE stabilization in the transition state compared to the ground state.
By understanding primary, secondary, and inverse KIEs, chemists can gain valuable mechanistic insights into both chemical and enzymatic reactions. Would you like specific reaction diagrams or further elaboration on enzyme-related KIEs?