Hemin-Graphene Derivatives with Increased Peroxidase Activities Restrain Protein Tyrosine Nitration

Graphical Selective oxidation : Hemin-graphene derivatives are synthesized. They show a pronounced effect on weakening protein tyrosine nitration. In addition, it is demonstrated that the hemin-graphene derivatives accelerate tyrosine (Tyr) and nitrite oxidation, but suppress the free-radical coupling reaction (see figure). Protein tyrosine nitration is implicated in the occurrence and progression of pathological conditions involving free radical reactions. It is well recognized that hemin can catalyze protein tyrosine nitration in the presence of nitrite and hydrogen peroxide. Generally, the catalytic efficiency is positively correlated to its peroxidase activity. In this study, however, it is found that the efficiency of hemin in catalyzing protein tyrosine nitration is largely suppressed after functionalization with graphene derivatives, even though its peroxidase-like activity is more than quadrupled. Further studies show that the oxidation of tyrosine is still observed for these composites; dityrosine formation, however, is greatly inhibited. Furthermore, these composites also exhibit strong effects on the oxidation of nitrite into nitrate. Therefore, we propose a mechanism in which hemin-graphene derivatives facilitate the oxidation of tyrosine and nitrite to produce tyrosyl radicals and nitrogen dioxide radicals in the presence of hydrogen peroxide, but graphene interlayers serve as barriers that hinder radical–radical coupling reactions; consequently, protein tyrosine nitration is restrained. This property of hemin-graphene derivatives, by which they catalyze substrate oxidation but suppress radical–radical coupling reactions, shows their great potential in selective oxidation procedures for byproduct removal.