Novel enzymatic oxidation of Mn2+ to Mn3+ catalyzed by a fungal laccase.
Fungal laccases are extracellular multinuclear copper-containing oxidases that have been proposed to be involved in ligninolysis and degradation of xenobiotics. Here, we show that an electrophoretically homogenous laccase preparation from the white rot fungus Trametes versicolor oxidized Mn2+ to Mn3+ in the presence of Na-pyrophosphate, with a Km value of 186 microM and a Vmax value of 0.11 micromol/min/mg protein at the optimal pH (5.0) and a Na-pyrophosphate concentration of 100 mM. The oxidation of Mn2+ involved concomitant reduction of the laccase type 1 copper site as usual for laccase reactions, thus providing the first evidence that laccase may directly utilize Mn2+ as a substrate.
Höfer
C
C
Friedrich-Schiller-University of Jena, Institute of Microbiology, Germany.
Schlosser
D
D
D011756:Diphosphates / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D005658:Fungi / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D042845:Laccase; D008345:Manganese / Q000378:metabolism*; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D012969:Sodium Fluoride / Q000494:pharmacology; D013997:Time Factors
D011756:Diphosphates; D008345:Manganese; D012969:Sodium Fluoride; D010088:Oxidoreductases; D042845:Laccase; C003319:sodium pyrophosphate