L-DOPA Dioxygenase (LmbB1) is the representative member of a distinct class of biosynthetic extradiol dioxygenases from the vicinal-oxygen-chelate superfamily. Originally identified from Streptomyces lincolnensis as part of the biosynthetic pathway to the antibiotic lincomycin, this class of enzymes can utilize FeII and molecular oxygen to cleave a variety of substrate analogs, including dopamines and 3,4-dihydroxydihydrocinnamic acids (DHHCAs). In order to investigate the L-DOPA dioxygenase mechanism as a function of substrate structure, a series of 6-substituted DHHCA derivatives were synthesized to explore a range of substrate pKa and redox potential. The synthetic, 6-substituted DHHCA derivatives were examined as enzymatic substrates using a combination of steady-state and stopped-flow spectroscopy. Effects of ring substituents on the enzymatic reaction pathway are discussed.

Synthetic derivatives of 3,4-dihydroxydihydrocinnamic acid as mechanistic probes of L-DOPA dioxygenase

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