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University of Illinois at Urbana-Champaign

Mechanistic Studies and Synthetic Applications of Phosphite Dehydrogenase

Abstract

dc:description

Cytochrome c oxidase, an enzyme that catalyzes the reduction of oxygen to water, has a binuclear center as well as a unique post-translational modification in the active site. Specifically, there is a crosslink between the nitrogen (Nepsilon2) of His240 and the carbon (Cepsilon 2) of Tyr244 (numbers correspond to CcO from bovine heart). The significance of the linkage was investigated by comparing the physicochemical properties of a model compound, 2-(imidazolyl-1-yl-4-methylphenol) to p-cresol.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Chemistry
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Vrtis, Jennifer Marie
Contributors dc:contributor
  • van der Donk, Wilfred A.

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI3070466
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/84091

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Vrtis, Jennifer Marie. Mechanistic Studies and Synthetic Applications of Phosphite Dehydrogenase. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/84091