Plant oxidoreductase enzymes have been widely used for their chemical versatility. They are used in many analytical schemes due to their robust catlysis, substrate promiscuity, and the ease with which their colorimetric or fluorometric probes can be monitored.. However, there may be drawbacks to such vast catalytic activity when undesired side reactions occur. We have found that plant peroxidases are capable of using a wide array of alcohols in their catlytic cycle to reduce various colorimetric and fluorormetric substrate probes. These alcohols pose a unique risk of contamination in various laboratory based assays and could result in false positives in clinical chemistry settings. The results of the biochemical characterization of the reactions of these peroxidases with various probes and alcohol substrates will be presented as well as insight gained into the mechanistic details of this off-target" biochemical activity.

Alcohol mediated oxidation of colorimetric and fluorometic probes by plant peroxidases

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.