Identification and Spectroscopic Characterization of the Active Sites of Two Class II Chelatases
Conference Year
2023
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.
Primary Faculty Mentor Name
Matthew Liptak
Graduate Student Mentors
Jacob Morris
Status
Undergraduate
Student College
College of Arts and Sciences
Program/Major
Chemistry
Primary Research Category
Physical Science
Identification and Spectroscopic Characterization of the Active Sites of Two Class II Chelatases
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.