Interactions of Gallic Acid with Porcine Hemoglobin: Effect on the Redox State and Structure of Hemoglobin.

Abstract

The effect of gallic acid (GA) on the redox state of hemoglobin (Hb) and the structural mechanism upon the Hb-GA interaction were investigated. Results indicated that GA exhibited antioxidant and pro-oxidant effects on Hb, which depended on its concentration and the redox state of Hb. The antioxidant capacity of GA contributed to the inhibition of free iron release from Hb. GA could bind to the central cavity of Hb and interacted with the heme moiety through direct hydrophobic contacts as indicated by docking analysis, but GA did not disrupt the heme structure. Conversely, GA increased the compactness of the Hb molecule and might narrow the crevice around the heme pocket, which contributed to the inhibition of Hb autoxidation and the free iron release. Results provided significant insights into the interaction of GA with redox-active Hb, which is beneficial to the application of GA in relative meat and blood products.