Isolation and characterization of a cysteine dioxygenase model complex intermediate from aqueous media

Abstract

Cysteine Dioxygenase (CDO) oxidizes cysteine to maintain homeostasis. Increased levels of cysteine have been linked to the development of neurological disorders, such as Alzheimer’s and Parkinson's, and autoimmune diseases, such as lupus and rheumatoid arthritis. This research aims to develop an isolation procedure for the intermediate and to study the binding mode of the intermediate in the absence of an arginine residue. Data was collected to determine the properties of the intermediate as well as whether the binding mode differs in the absence of the arginine residue or remains the same as CDO.