Abstract

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 natural products as well as degrade plant material, but we have a limited understanding of substrate space and mechanism across the superfamily. To this end, we report the syntheses, redox potentials and pKas of L‐3,4‐dihydroxyphenylalanine (L‐DOPA) derivatives substituted at the 6‐position and their characterization as substrates of L‐DOPA dioxygenase from lincomycin biosynthesis in Streptomyces lincolnensis. In particular, the spectroscopic properties of 6‐nitroDOPA provide insight into the steps of the enzymatic mechanism. The applications for dioxygenase cleavage of 6‐substituted L‐DOPA derivatives to natural product biosynthesis will be discussed.

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