Dioxygenase enzymes are nature’s catalysts for the breakdown of catecholic rings, such as those found in the woody tissue of plants. This chemistry has tremendous potential not only in the degradation of plant material, but also in natural product biosynthesis. A suite of synthetic dopamines, derivatized at the 6-position and varied in substituent size and electron-withdrawing character, were examined as substrates of S. lincolnensis L-DOPA dioxygenase via in-silico docking and subsequent analysis of the enzyme catalyzed transformations by mass spectrometry and UV-Visible spectroscopy. 6-bromodopamine, 6-cyanodopamine and 6-carboxydopamine were robust substrates, while cyclicdopamine and 6-nitrodopamine exhibited limited turnover. Docking and kinetic experiments are used to explain these substrate preferences by L-DOPA dioxygenase.

6-substituted derivatives of dopamine as substrates of L-DOPA dioxygenase: Understanding steric and electronic substituent effects

ACS Fall 2021

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