Date of Award

Spring 2020

Degree Type

Thesis

Department

Chemistry and Biochemistry

Director of Thesis

Thomas Makris, PhD

Second Reader

Hippokratis Kiaris, PhD

Abstract

The overall structure and ligand arrangement of diiron enzymes influence their function and catalytic potential, allowing for them to catalyze an expansive breadth of high energy transformations. The diiron enzyme CADD from Chlamydia trachomatis is involved in a novel biosynthetic pathway for p-aminobenzoic acid (pABA), a precursor for tetrahydrofolate. The unique ligand structure and reactivity of CADD and homolog NE1434 provide an intriguing means to contrast structure function relationships with other known diiron enzymes that activate dioxygen. In this work, studies of CADD and NE1434 orthologs and comparison to other diiron enzymes reveal several sequence motifs that are likely critical for its distinct function.

First Page

1

Last Page

26

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