Publication Date

1-1-2014

Document Type

Dissertation/Thesis

First Advisor

Meganathan, Rangaswamy

Degree Name

B.S. (Bachelor of Science)

Legacy Department

Department of Biological Sciences

Abstract

An essential component of the respiratory chain of aerobic prokaryotes and eukaryotes is Conezyme Q (Ubiquinone, Q), which acts as an electron carrier thereby serving as a link between dehydrogenases and the subsequent electron acceptors in the respiratory chain. In Escherichia coli, during Q biosynthesis, the decarboxylation step is catalyzed by two isofuncational enzymes, UbiD and UbiX. UbiD carries out the decarboxylation of 80% of the substrate, 3-octaprenyl-4-hydroxybenzoate whereas UbiX is responsible for the remaining 20%. It has been reported that the loss of UbiX decreases UbiG O- methyltransferase activity by .36 fold and the growth in Luria-Bertani (LB) broth as well as in succinate minimal medium is severely affected. Contrary to this report, we discovered that the deltaUbiX mutant grows to wild-type levels in both media and synthesizes close to wild-type levels of Q.

Extent

12 pages

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

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