University of Illinois Urbana-Champaign

Mechanistic Studies and Synthetic Applications of Phosphite Dehydrogenase

Vrtis, Jennifer Marie

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Description

Title
Mechanistic Studies and Synthetic Applications of Phosphite Dehydrogenase
Author(s)
Vrtis, Jennifer Marie
Issue Date
2002
Doctoral Committee Chair(s)
van der Donk, Wilfred A.
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Organic
Language
eng
Abstract
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.
Graduation Semester
2002
Type of Resource
text
Permalink
http://hdl.handle.net/2142/84091

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