Simulation Studies of Aromatic Amine Dehydrogenase bound Phenylethylamine Analogues

  • Philip Peartree

Student thesis: Phd


A series of para-substituted phenylethylamine analogues bound to the enzyme aromatic amine dehydrogenase have been simulated using quantum mechanical electronic structure calculations and molecular mechanical molecular dynamics simulations. Trends have been verified connecting bond dissociation energy (and thus driving force) to observed rate constants and activation enthalpy. Trends have been identified in connecting statistics drawn from molecular dynamics simulations and the temperature dependence of the kinetic isotope effect, notably that as the temperature dependence of the kinetic isotope effect increases the flexibility of the promoting vibration decreases. This is explained as being more effected by thermal energy put into the system, and therefore more affected by temperature.
Date of Award31 Dec 2011
Original languageEnglish
Awarding Institution
  • The University of Manchester
SupervisorMichael Sutcliffe (Supervisor)


  • Quantum Mechanics
  • Enzymology
  • Computational Chemistry
  • Molecular Dynamics
  • Hydrogen Tunneling
  • Aromatic Amine Dehydrogenase
  • Quantum Tunneling
  • AADH

Cite this