Masters Theses

Date of Award

8-2008

Degree Type

Thesis

Degree Name

Master of Science

Major

Chemical Engineering

Major Professor

Paul D. Frymier

Committee Members

Barry Bruce, Eric Boder

Abstract

A mutant form of the protein complex cytochrome c553 (cyt c553) has been constructed by site-directed mutagenesis in Thermosynechococcus elongatus (T. elongates) to elucidate the binding and electron transfer properties between cyt c553 and photosystem I (PSI). The electron-transfer between wild type T. elongatus cyt c553 and a mutant form of cyt c553 and T. elongatus and Chlamydomonas reinhardtii (C. reinhardtii) PSI, has been studied as a function of cyt c553 concentration, ionic strength, pH and the detergents used to stabilize the protein. The effects of each of these variables were measured by an oxygen uptake assay. The mutated T. elongatus cyt c553 shows a higher electron transfer rate to C. reinhardtii PSI indicating that the insertion of acidic residues to the protein has facilitated the electrostatic interactions between cyt c553 and PSI. The effects of ionic strength and pH on the reaction indicate a strong influence of complementary charges on complex formation and stabilization.

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