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 powerful enzymes. To this end, we report the syntheses, redox potentials and pKas of 3,4-dihydroxyhydrocinnamic acid (DHHCA) derivatives substituted at the 6-position and their characterization as substrates of L-DOPA dioxygenase from Streptomyces lincolnensis. The cleavage of diverse catecholic substrates is an important element of bioremediation. Extradiol dioxygenase cleavage of DHHCA derivatives also promises to yield insight into mechanism and provide synthons for various applications.
