8-Oxo-7,8-dihydroguanosine (8-oxoG) is a result of oxidative damage on the nucleobase Guanosine. 8-OxoG has been well characterized in DNA, but little is known of its function in RNA. The purpose of this study was to understand how 8-oxoG influences enzyme reactivity, RNA structure, and RNA function. First, endoribonucleases Ribonuclease A (RNase A) and Ribonuclease T₁ (RNase T₁) were studied to understand 8-oxoG recognition. It was found that 8-oxoG becomes a substrate for RNase A, while it was not recognized by RNase T₁. The functional group on C8 causes an anti to syn flip which exposes new hydrogen bonding patterns similar to that of Uridine, which allowed RNase A reactivity. The conformational change, though, causes 8-oxoG to lose its ability to be a substrate for RNase T₁ due to sterics and adverse hydrogen bonding induced by the exocyclic functional group at C8. The information gathered from the endoribonucleases was then applied to study how 8-oxoG begets structural and functional changes to a well-studied aptamer, the theophylline binding aptamer. 8-OxoG insertion caused a 100-fold increase in dissociation constant (K_d) for the theophylline binding aptamers modified at positions G25 and G26, while a modification at G11 prevented the aptamer from binding to theophylline. RNase A and T₁ degradation data also yielded different degradation sites in the modified aptamers compared to the canonical, indicating a change in structure. Following, the reactivity of exoribonuclease XRN1 was studied in the presence of oligomers containing one to three 8-oxoG modifications due to XRN1’s role in oxidized mRNA surveillance. XRN1 was found to stall at 8-oxoG sites as a function of number of 8-oxoG present when more than one modification was introduced. The data combined helps provide insights into how 8-oxoG may affect RNA decay and surveillance mechanisms.