(-)-Epigallocatechin gallate as an inhibitor of hemoglobin-catalyzed lipid oxidation: molecular mechanism of action and nutritional application

Hemoglobin (Hb) is effective inducer for lipid oxidation and protein-polyphenol interaction is a well-known phenomenon. The effects of the interaction of (-)-epigallocatechin gallate (EGCG) with Hb on lipid oxidation were rarely elucidated. The detailed interaction between bovine Hb and EGCG was systematically explored by experimental and theoretical approaches, to illustrate the molecular mechanisms by which EGCG influenced the redox states and stability of Hb. EGCG would bind to the central pocket of protein with one binding site to form Hb-EGCG complex. The binding constant for Hb-EGCG complex was 0.34 x 10(4) M-1 at 277 K, and thermodynamic parameters (Delta H > 0, Delta S > 0 and Delta G < 0) revealed the participation of hydrophobic forces in the binding process. The binding of EGCG would increase the compactness of protein molecule and diminish the crevice near the heme cavity, which was responsible for the reduction of met-Hb to oxy-Hb and inhibition of hemin release from met-Hb. Moreover, EGCG efficiently suppressed Hb-caused lipid oxidation in liposomes and cod muscles, which was possibly attributed to the reduction to oxy-Hb state and declined hemin dissociation from met-Hb. Altogether, our results provide significant insights into the binding of EGCG to redox-active Hb, which represents a novel mechanism for the anti-oxidant capacity of EGCG in human health and is favorable to the applications of natural EGCG in the good quality of Hb-containing products.