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Title:Structure-Function Relationship Studies of the Rhodobacter Sphaeroides Cytochrome AA(3)
Author(s):Lee, Hang Mo
Doctoral Committee Chair(s):Gennis, Robert B.
Department / Program:Chemistry
Discipline:Chemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Chemistry, Biochemistry
Abstract:Cytochrome c oxidases catalyze the reduction of O2 to H 2O and use the redox energy released by this reaction to generate an electrochemical proton gradient. This proton gradient can be used to produce ATP by ATP-Synthase. Rhodobacter sphaeroides cytochrome c oxidase, the focus of this thesis, serves as an excellent model to systematically understand the more complicated mammalian cytochrome c oxidases. The role of a putative proton channel identified in the X-ray crystal structure of the cytochrome c oxidases from bovine heart mitochondria and P. denitrificans has been studied using site-directed mutagenesis coupled with a variety of biophysical characterization methods. Based on the work done, it is concluded that the putative proton channel is not functional in prokaryotic oxidases. A hydrogen bond responsible for a large red shift in the visible spectrum of cytochrome c oxidases compared to that of model heme compounds has been identified and characterized through site-directed mutagenesis and resonance Raman spectroscopy. Residues coordinating the calcium ion in R. sphaeroides cytochrome c oxidase have been mutated to mimic the metal binding site of bovine mitochondrial oxidase. Residues in a putative oxygen channel to the active site have been mutated and characterized. It was observed that only the mutations near the active site hinder oxygen binding.
Issue Date:2001
Type:Text
Language:English
Description:170 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001.
URI:http://hdl.handle.net/2142/84025
Other Identifier(s):(MiAaPQ)AAI3017140
Date Available in IDEALS:2015-09-25
Date Deposited:2001


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