Subject Area
Chemistry
Description
The bacteria of the human gut microbiome can metabolize drugs, often causing unintended side effects. The uniqueness and variability of each individual’s microbial composition, coupled with our limited understanding of specific enzyme functions, make the metabolic outcomes of these therapeutics difficult. Azoreductase enzymes are of particular interest due to their ability to reduce azo bonds, which are often found in drugs and food dyes. Azo dyes can also be reduced nonenzymatically by hydrogen sulfide, a bacterial metabolite produced during sulfate and cysteine metabolism. The goal of this study is to examine the specificity and relative kinetics of both enzymatic and nonenzymatic reduction of azo compounds by synthesizing and characterizing a library of 32 structurally diverse azo- bonded molecules with varying electronic properties. These compounds fall into three main groups, each of which is designed to test our proposed azoreductase mechanism. We hypothesize that azoreductases do not directly reduce azo bonds but instead reduce quinone-like tautomers of azo compounds. Out of the 32 compounds, 16 have been synthesized, and the reduction potential of 12 has been measured. The reduction potentials ranged from -1.138 V to - 0.672 V among the phenylazophenol derivatives and from - 0.911 V to -0.567 V for the benzenesulfonic acid-based azo compounds, highlighting clear electronic effects on reduction behavior. Other members of our research group are determining the enzymatic rate of reduction of these compounds. These findings broaden our understanding of microbial azo reduction, helping to develop safer therapeutics for treating diseases of the large intestine and supporting future personalized medicine
Publisher
Providence College
Date
Spring 4-22-2026
Start Date
4-22-2026 11:00 AM
Type
Poster
Format
Text
.pdf (text under image)
Language
English
