The activated complex in chemical reactions

Eyring, H. (1935). The activated complex in chemical reactions. The Journal of Chemical Physics, 3(2), 107-115.

Type

Journal article

Intellectual base

Primary research

Year

1935

DOI

10.1063/1.1749604

Link

https://doi.org/10.1063/1.1749604

Cited from

chemistry_materials, mathematics, physics

Cited by

3 citations across 3 artifacts.

Each citation links to the sentence it supports in the citing article.

Primes

• Activation Energy
  • It separates two states (unreacted and reacted; dormant and active; fragmented and mobilized) and names the work required to cross between them.

    This sourceFoundational paper on transition state theory: formalizes the barrier-threshold-transition structural pattern via the activated complex in quasi-equilibrium with reactants. SUPPORTS the structural-signature claim that the pattern was formalized in Eyring's transition state theory.

• Hidden Path and Barrier Crossing
  • This quantum-mechanical contribution is particularly important in enzymes like monoamine oxidase, alcohol dehydrogenase, and methylamine dehydrogenase, where hydrogen or deuterium kinetic isotope effects (H/D KIE values >> 1) directly indicate tunneling.

    This sourceFoundational paper on transition state theory: formalizes the barrier-threshold-transition structural pattern via the activated complex in quasi-equilibrium with reactants.

• Saddle Point
  • Theoretical ecology characterized coexistence equilibria by which directions are stable, an analysis identical in form to dynamical-systems saddles, and chemistry found that reaction transition states are saddles of the potential-energy surface, the same geometry driving Eyring's transition-state theory.

Verification

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