Structure-Function Relationship Studies of the Rhodobacter Sphaeroides Cytochrome AA(3)
Lee, Hang Mo
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https://hdl.handle.net/2142/84025
Description
Title
Structure-Function Relationship Studies of the Rhodobacter Sphaeroides Cytochrome AA(3)
Author(s)
Lee, Hang Mo
Issue Date
2001
Doctoral Committee Chair(s)
Gennis, Robert B.
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, Biochemistry
Language
eng
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.
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