Analysis of FeSOD from E. coli

Abstract

Due to their central position in various physiological conditions, and their involvement in a broad range of diseases, the importance of free radicals in biology has increased dramatically in recent years. Scientists have shown great interest in investigating the roles these radicals perform in illness, and how they counteract the normal physiological environment. In 1954, Gershman first proposed the idea that the toxicity of oxygen is due to its capacity to produce free radicals. Via their study, Commoner et al (1954) confirmed that in the same year free radicals appeared in biological materials. Superoxide dismutase (EC 1.15.1.1) is an enzyme that alternately catalyses dismutation of superoxide to molecular oxygen (O2) and hydrogen peroxide (H2O2) (Sheng et al., 2014). Superoxide is a by-product of oxygen metabolism that causes all kinds of cell damage when left unregulated. The aim of this research was to attempt to analyse the activity of 2 mutant proteins; FeSOD dblDGF and FeSOD MIH to potentially gain further understanding of the key residues that are important for protein selectivity and specificity. The results from testing showed that FeSOD dblDGF elicited 35% activity relative to wild type FeSOD, whilst FeSOD MIH showed almost no activity at all. Given the limited testing, it was impossible to ascertain what is happening structurally or chemically to these proteins, so the activity exhibited by these proteins cannot be fully explained or accounted for, in terms of specificity and selectivity, using this research data alone.