<br/>L-DOPA dioxygenase is predicted to 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, steady-state and pre-steady state activities of mutant L-DOPA dioxygenases were examined as a function of pH and substrate concentration.

Using pre-steady state and steady-state kinetics to examine the roles of active site residues in L-DOPA dioxygenase

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.