The lactococcal multidrug resistance regulator (LmrR) transcription factor protein from Lactococcus lactis has been used as a scaffold to enhance the regio- and enantioselectivity of multiple copper-catalyzed reactions, and most recently, hemin-catalyzed cyclopropanation. Spectroscopic and crystallographic data indicate that the hemin-cofactor is tightly bound to the hydrophobic pore of LmrR via interactions with two tryptophan residues, while dynamics simulations reveal considerable conformational flexibility to allow for substrate binding and catalysis. In this work, we report on the peroxidase activity of the hemin-LmrR complex and describe efforts to further improve this activity via site-directed mutagenesis.<br/>

Enhancement of peroxidase activity in a hemin-based artificial enzyme

2019 Spring National Meeting

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