Due to the advancements in cancer treatment and increasingly prevalent antibiotic-resistant bacteria, the CDC estimates that by the year 2050, deaths from bacterial infections will surpass annual casualties from cancer. A tactic commonly used in antibiotic drugs is to damage infecting organisms at Fe-S clusters through Reactive nitrogen species, usually in the form of NO. Bacteria, in turn, have developed a response pathway resulting in the upregulation of repair iron cluster (RIC) metalloproteins. Among RIC proteins, the E. coli protein, YtfE, is one of the best characterized. YtfE is capable of both mitigating nitrosative stress and repairing damage done by reactive species though the mechanisms though the mechanisms of the processes are unknown. Here, we explore the kinetics of NO reduction by YtfE. The rate of depletion of the substrate, NO, and formation of oxidized YtfE was tracked by UV-vis spectroscopy and fit to Michaelis-Menten and Lineweaver-Burke kinetic curves in the program MATLAB. The Km and kcat for NO reduction were calculated and compared to nitric oxide reductase. The results suggest that the reduction of NO is not the primary function of YtfE.

Steady-state kinetics of E. coli YtfE nitric oxide reduction

ACS Spring Meeting 2021

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.