Reactivity of cuprous stellacyanin as a quinone and semiquinone reductase.
The reactivity of cuprous stellacyanin as a quinone and semiquinone reductase has been examined. Rate constants (25.0 degrees C) measured for the oxidation of stellacyanin by 1,4-benzoquinone and benzosemiquinone are 2.3 X 10(4) M-1 s-1 (delta H not equal to = 4.4 kcal/mol, delta S not equal to = -24 eu) and 5.1 X 10(6) M-1 s-1, respectively [pH 7.0, I = 0.1 M (phosphate)]. The agreement of these rate constants with those calculated on the basis of relative Marcus theory is discussed. Stellacyanin is more effective than laccase in quenching benzosemiquinone, suggesting that the physiological role of this metalloprotein is to regulate the concentration of free radicals generated through the laccase-catalyzed oxidation of phenols.
D002151:Calorimetry; D007700:Kinetics; D008433:Mathematics; D008667:Metalloproteins / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010947:Plants, Toxic; D011808:Quinone Reductases / Q000378:metabolism*; D012251:Toxicodendron
D008667:Metalloproteins; D010940:Plant Proteins; C003343:stellacyanin protein, plant; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases