Dioxygenase enzymes are essential protein catalysts for the breakdown of catecholic rings, structural components of plant woody tissue. This powerful chemistry is used in nature to make antibiotics and other bioactive materials as well as degrade plant material, but we have a limited understanding of the breadth and depth of substrate space for these enzymes. To this end, we report the synthesis of dopamine derivatives substituted at the 6-position with various electron-donating or withdrawing substituents and their characterization as substrates of L-DOPA dioxygenase. The cleavage of diverse catecholic substrate is an important element of bioremediation, and extradiol dioxygenase cleavage of dopamine derivatives promises to yield synthons for various applications. <br/>

Probing substrate space in dioxygenase catalysis: Investigation of 6-substituted dopamine derivatives as substrates of L-DOPA dioxygenase

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.