COMING SOON! PQDT Open is getting a new home!

ProQuest Open Access Dissertations & Theses will remain freely available as part of a new and enhanced search experience at

Questions? Please refer to this FAQ.

Dissertation/Thesis Abstract

Investigation of the Temperature Dependence of Primary Kinetic Isotope Effects of Hydride Transfer Reactions in Solution
by Maness, Peter, M.S., Southern Illinois University at Edwardsville, 2019, 103; 22591975
Abstract (Summary)

The purpose of this research is to investigate the quantum mechanical concept of tunneling in hydride-transfer reactions in solution. It is to support the contemporary Marcus-like H-tunneling model and further support the concept of donor-acceptor distances (DAD) about the tunneling-ready-state (TRS). The change from the temperature independence of the primary (1°) H/D kinetic isotope effects (KIEs) in wild-type enzyme-catalyzed H-transfer reactions (∆Ea = EaD - EaH ~ 0) to strong temperature dependence with the mutants (∆Ea >> 0) have recently been frequently observed. We study the structural effects on the temperature dependence of primary (1°) KIEs for H-transfer reactions in solution in an attempt to compare with well-studied enzymatic H-transfer reactions. The hypothesis is that a greater temperature dependence of 1° KIEs should be observed in H/D-transfer reaction systems that have a loosely associated TRS, which allows donor-acceptor distance (DAD) sampling. Hydride transfer reactions from several dihydropyridines to various hydride acceptors, in acetonitrile, were studied to investigate this hypothesis. The relationship between structures and ΔEa(D-H) are compared for reactions in solution vs. enzymes. The reactions take place by an H-tunnelling mechanism, irrespective of the reaction media. It appears that the more rigid donor-acceptor complexes that are more sterically hindered and more tightly associated would give rise to a weaker temperature dependence of 1° KIEs. This is consistent with the trend observed in wild-type enzymes vs. mutants, in which the active site of the wild-type enzyme is tightly packed and does not readily allow DAD sampling, thus resulting in weak temperature dependence of 1° KIEs. Our results replicate the enzyme observations and support the new concept that the local thermal motions promote the enzyme catalysis.

Indexing (document details)
Advisor: Lu, Yun
Commitee: Luesse, Sarah, O'Brien, Leah
School: Southern Illinois University at Edwardsville
Department: Chemistry
School Location: United States -- Illinois
Source: MAI 81/3(E), Masters Abstracts International
Subjects: Chemistry
Keywords: Tunneling-ready-state, Donor-acceptor distances, H-transfer reactions
Publication Number: 22591975
ISBN: 9781088374252
Copyright © 2021 ProQuest LLC. All rights reserved. Terms and Conditions Privacy Policy Cookie Policy