Catecholic rings are structural components of the woody tissue of plants. Dioxygenase enzymes are essential protein catalysts for the breakdown of catecholic rings. 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 structure-function relationship in these enzymes. L-DOPA dioxygenase is predicted bind iron at the interface of two subunits using two histidine residues and a glutamate residue from different subunits. A neighboring tyrosine and histidine are also proposed to participate in catalysis. To investigate the roles of these active-site residues, activity of mutant L-DOPA dioxygenases was correlated with the iron content quantified with a calibrated FerroZine assay.

Evaluating the roles of active-site residues in catalysis and iron-binding in L-DOPA dioxygenase

2019 Spring National Meeting

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