Degree Name
MS (Master of Science)
Program
Biology
Date of Award
5-2011
Committee Chair or Co-Chairs
Michael S. Zavada
Committee Members
Hugh A. Miller III, Karl H. Joplin
Abstract
ATP Synthase is the fundamental means of cellular energy production in animals, plants, and almost all microorganisms. In order to understand the mechanism of ATP catalysis, critical amino acid residues involved in Pi binding have to be identified. The αVISIT-DG sequence at the interface of α/β subunits that contains residues from 345-351 is highly conserved and αAsp-350 has been chosen because of its negative charge side chain and its close proximity (~2.8 Å) to the known phosphate binding residue αArg-376. The mutant's αD350R, αD350Q, αD350A, αR376A/D, and αG351R/A/D were generated by site directed mutagenesis and several biochemical assays were performed on them to understand the role played by the amino acid residues in Pi binding. Biochemical results suggest that αD350 may be involved in catalysis of ATP synthase and play an important role in Pi binding, whereas αG351 may be involved only in the structural integrity.
Document Type
Thesis - unrestricted
Recommended Citation
Jonnalagadda, Sneha R., "Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of Escherichia coli ATP Synthase." (2011). Electronic Theses and Dissertations. Paper 1296. https://dc.etsu.edu/etd/1296
Copyright
Copyright by the authors.