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 large consumer of manganese ores. Scheele and other chemists were aware that manganese dioxide contained a new element, but they were not able to isolate it. Johan Gottlieb Gahn was the first to isolate an impure sample of manganese metal in 1774, by reducing the dioxide with carbon. The manganese content of some iron ores used in Greece led to speculations that steel produced from that ore contains additional manganese, making the Spartan steel exceptionally hard. Around the beginning of the 19th century, manganese was used in steelmaking and several patents were granted. In 1816, it was documented that iron