Identification and Spectroscopic Characterization of the Active Sites of Two Class II Chelatases
Lavigne, Megan
Lavigne, Megan
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Abstract
Class II chelatases are enzymes that selectively insert divalent transition metals into tetrapyrroles, which are precursors to a group of biological cofactors. Although these metalated tetrapyrroles are essential to many of life’s biological processes, the specificity of metal insertion in their biosynthesis is still unknown. Determining the active site structure of these enzymes and their interaction with metals, through spectroscopic characterization and site-directed mutagenesis, will help to determine the origin of selective metal insertion. Understanding the metal selectivity of these tetrapyrroles’ biosynthesis can ultimately result in the design of synthetic chelatases to biosynthesize non-natural metal tetrapyrroles that catalyze energy-conversion reactions.
Description
Undergraduate
Date
2023-01-01
