[Comparative kinetics of reactions catalyzed by glucose oxidase in the presence of different electron acceptors].
It was shown that six redox indicators, beside oxygen, can be used as substrates for glucose oxidase from Penicillium vitale. The pH dependence of the rate of glucose oxidase-catalyzed reactions in the presence of oxygen and artificial electron acceptors was studied. In contrast to the reaction involving oxygen, in which the maxima of the pH activity profile were observed at pH 5.6, glucose oxidase reveals maximal pH activity profile at pH 7.5 -- 7.6 in the presence of phenasine methosulfate, basic dark-blue 2K, viologens and ion-radical salt of N,N,N',N'-tetramethyl-rho-phenylene diamine. It was assumed that there exist two forms of the reduced enzyme differing in their rates of oxidation by oxygen and in ability to reduce artificial electron acceptors via one-electron transfer.
D004396:Coloring Agents; D004579:Electron Transport; D005949:Glucose Oxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010084:Oxidation-Reduction; D010407:Penicillium / Q000201:enzymology*
D004396:Coloring Agents; D005949:Glucose Oxidase
Sravnitel'noe izuchenie reaktsiĩ, kataliziruemykh gliukozooksidazoĩ v prisutstvii razlichnykh aktseptorov elektronov.