Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata.
A homogeneous Mn-dependent peroxidase (MnP) was purified from the extracellular culture fluid of the lignin-degrading white rot fungus Phlebia radiata by anion exchange chromatography. The enzyme had a molecular weight of 49,000 and pI 3.8. It was a glycoprotein, containing carbohydrate moieties accounting for 10% of the molecular weight. Mn-peroxidase was capable of oxidizing phenolic compounds in the presence of H2O2, whereas the effect on nonphenolic lignin model compounds was insignificant. MnP contained protoporphyrin IX as a prosthetic group. During enzymatic reactions H2O2 converted the native MnP to compound II. Mn2+ was essential in completing the catalytic cycle by returning the enzyme to its native state. The oxidation of ultimate substrates was dependent on superoxide radicals, O2- and probably on Mn3+ generated during the catalytic cycle. MnP exhibited high activity of NADH oxidation without exogenously added H2O2. It was shown to produce H2O2 at the expense of NADH.
Karhunen
E
E
VTT, Biotechnical Laboratory, Espoo, Finland.
Kantelinen
A
A
Niku-Paavola
M L
ML
D005658:Fungi / Q000032:analysis*; D007525:Isoelectric Focusing; D008031:Lignin / Q000378:metabolism*; D009243:NAD; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000302:isolation & purification*; D011489:Protein Denaturation; D013053:Spectrophotometry
D009243:NAD; D008031:Lignin; D010544:Peroxidases; C051129:manganese peroxidase