Non enzymatic covalent modification by glycolysis end product converts hemoglobin into its oxidative stress potency state.

The effect of glycation by Pyruvic acid (PA) on the early and advanced conformational changes in Hemoglobin (Hb) was studied. Multi Spectroscopic measurement revealed that Hb undergoes structural conformational changes and unbound heme upon incubation with PA. These covalent modifications were followed by the reduction of heme centre and these reduction processes initiates its peroxidase-like activity. An extended PA glycation resulted in the appearance of advanced glycation end products fluorescence, with notable changes in compositions of secondary structure. The amyloidogenic state was confirmed by SEM, fluorescence microscope observation. This study reveals an insight to the role of pyruvic acid which increases the oxidative stress due to the heme reduction and diabetic complication.