Manganese peroxidase Manganese peroxidase In enzymology, a manganese peroxidase () is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are Mn(II), H, and HO, whereas its two products are Mn(III) and HO. This enzyme belongs to the family of oxidoreductases, to be specific those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is Mn(II):hydrogen-peroxide oxidoreductase. Other names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing) peroxidase. It employs one cofactor, heme. This enzyme needs Ca for activity. White rot fungi secrete this enzyme to aid lignin degradation. Manganese peroxidase (commonly referred
Manganese to be manganese dioxide) contained a new element, but they were unable to isolate it. Johan Gottlieb Gahn was the first to isolate an impure sample of manganese metal in 1774, which he did by reducing the dioxide with carbon. Manganese phosphating is used for rust and corrosion prevention on steel. Ionized manganese is used industrially as pigments of various colors, which depend on the oxidation state of the ions. The permanganates of alkali and alkaline earth metals are powerful oxidizers. Manganese dioxide is used as the cathode (electron acceptor) material in zinc-carbon and alkaline batteries. In biology, manganese(II) ions