Metal containing enzymes play a crucial role in protecting cells from reactive oxygen species (ROS). These types of enzymes may function as antioxidants and are essential to the human body as oxidative stress can be damaging to cells thus having implications with cancer and certain types of neurodegenerative diseases. Biomimetic modeling is a way to study these enzymes by making synthetic analogues of the enzyme’s active site. Such studies are integral to understanding the enzyme’s functionality and mechanism of action. The focus of this project is Cu,Zn superoxide dismutase (SOD1), an enzyme responsible for scavenging the toxic superoxide radical produced during aberrant metabolism by catalyzing the dismutation of superoxide into molecular oxygen and hydrogen peroxide. Recent findings suggest aggregation of the copper sub-unit can cause the protein to act as an aberrant form of SOD1, which can be linked to neurodegenerative diseases such as familial amyotrophic lateral sclerosis (fALS). Notably, the electrostatic loop (ESL) of SOD1, a conserved cluster of charged residues, is said to be associated with the mobility of the copper binding site. More specifically, the ESL can act as a geometric breathing motion which allows for proper catalytic functionality by alternating conformations intermediate between planar Cu+ and tetra coordinated Cu2+ oxidation states. Loss of ESL mobility can cause the Cu2+ center to be stranded in a distorted planar geometry which can catalyze the binding of hydrogen peroxide to then lead to the formation of a bound hydroxyl radical. In an attempt to model the copper sub-unit of superoxide dismutase, a copper(II) complex was synthesized displaying a pseudo-planar arrangement between three donating ligands. The geometry of the complex was shown to be closely related to the aberrant Cu2+ intermediate form of a distorted CuSOD stranded planar arrangement. A family of copper(II) complexes with structurally related ligands and varying geometric distortions were synthesized and spectroscopically characterized. The redox behavior of these complexes and the implications of these studies on aberrant biomimetic reactivity behaviour will be discussed.

Investigating the structural and electrochemical properties of a family of biomimetic models for the Cu2+ aberrant state of Cu,Zn superoxide dismutase (SOD1)

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.