Advisor | Offenbacher, Adam R | |
Author | Ohgo, Kei | |
Date Accessioned | 2020-12-18T15:42:23Z | |
Date Available | 2020-12-18T15:42:23Z | |
Date Created | 2020-12 | |
Date of Issue | 2020-12-09 | |
xmlui.metadata.dc.date.submitted | December 2020 | |
Identifier (URI) | http://hdl.handle.net/10342/8794 | |
Description | Proton-coupled electron transfer plays an important role in substrate oxidation by C-H bond cleavage and long-range pathways associated with bioenergetics. This thesis is focused on the synthesis of unnatural substrates and tryptophan amino acids to study these effects in enzyme reactions. The functionalization of C-H bonds is an important chemical transformation, representing a challenge in the design of asymmetric organometallic catalysts to generate a range of organic molecules with diverse functional groups. Soybean lipoxygenase-1 is a model enzyme system that catalyzes C-H activation reactions. Unnatural and volume-filling fatty acid derivatives were designed to test with a mutant soybean lipoxygenase that has an expanded active site. The goal of this strategy is to develop new hydroperoxide-based products of long-chain aliphatic compounds. Fluorinated 5-hydroxytryptophan (Fn-5HOW) derivatives were synthesized on a large scale using a chemoenzymatic approach. These redox-active Fn-5HOW derivatives exhibit tyrosine-like proton-bound oxidation and are associated with the spectroscopic characteristics of neutral radicals that are easily distinguishable from natural aromatic amino acids. As a proof of concept, these unnatural amino acids have been incorporated into structured peptides and model proteins. These unnatural fluorinated 5HOW derivatives may act as reporters for tryptophan-mediated biological electron transport. | |
Mimetype | application/pdf | |
Language | en | |
Publisher | East Carolina University | |
Subject | Proton Coupled Electron Transfer | |
Library of Congress Subject Headings | Enzymes | |
Library of Congress Subject Headings | Charge transfer | |
Library of Congress Subject Headings | Amino acids | |
Library of Congress Subject Headings | Tryptophan | |
Library of Congress Subject Headings | Lipoxygenases | |
Title | DEVELOPMENT OF UNNATURAL SUBSTRATES AND TRYPTOPHAN AMINO ACIDS TO STUDY PROTON COUPLED ELECTRON TRANSFER IN ENZYMES | |
Type | Master's Thesis | |
xmlui.metadata.dc.date.updated | 2020-12-18T14:33:11Z | |
Department | Chemistry | |
xmlui.metadata.dc.degree.name | M.S. | |
xmlui.metadata.dc.degree.level | Masters | |
xmlui.metadata.dc.degree.discipline | MS-Chemistry | |
xmlui.metadata.dc.degree.grantor | East Carolina University | |
xmlui.metadata.dc.degree.department | Chemistry | |
xmlui.metadata.dc.access.option | Open Access | |
xmlui.metadata.dc.type.material | text | |