Nitric Oxide (NO) is a signaling molecule involved in many plant processes, including growth and stress management. NO is found in the cell as GSNO and GSNO levels are regulated by NADH-dependent, S-nitrosoglutathione reductase (GSNOR). We hypothesize that NO homeostasis is controlled, in part, by interactions between other proteins and GSNOR. Potential GSNOR interactors in Arabidopsis thaliana were previously identified from literature, in vitro data, and proximity labeling. Validating protein interactors with GSNOR is crucial to understanding how GSNOR is regulated in Arabidopsis thaliana. Three potential interacting proteins have been chosen to be the focus of this research: thioredoxin H5 (TrxH5), UDP-glycosyltransferase 75D1 (UGT75D1), and thioredoxin domain-containing protein 9 (TXND9). To validate the interaction of these proteins with GSNOR, co-immunoprecipitation assays will be performed. To determine the significance of these interactions, native GSNOR has been purified for use in direct protein interaction assays. These experiments will elucidate whether the protein interactions alter the activity of GSNOR and provide data about the strength of interaction. Another class of proteins, aldo-keto reductases 4C8-11 (AKR4Cs), will be explored as alternative GSNOR reductases. The localization and activities of these proteins in AKR4C mutants will be characterized to better understand their function. Together, these results provide a better understanding of how GSNOR activity is regulated through protein interactions and how GSNOR works with the AKR4C proteins to control NO homeostasis and dictate plant processes and responses.