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species: 750279
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notes: Default parameter values are those in the right hand panel of Fig 12. The other panels may be obtained by setting X to 1, 2 or 4, and K3 to 0, 1/2 or 1. This model is described in: The kinetics of the enzyme-substrate compound of peroxidase. Britton Chance, Journal of Biological Chemistry , 151, 553-577, 1943. PDF at JBC reprinted in: Adv Enzymol Relat Areas Mol Biol. 1999;73:3-23. PubmedID: 10218104 > Abstract: Under the narrow range of experimental conditions, and at a temperature of approximately 25 degrees, the following data were obtained. 1. The equilibrium constant of peroxidase and hydrogen peroxide has a minimum value of 2 x 10(-8). 2. The velocity constant for the formation of peroxidase-H2O2 Complex I is 1.2 x 10(7) liter mole-1 sec.-1, +/- 0.4 x 10(7). 3. The velocity constant for the reversible breakdown of peroxidase-H2O2 Complex I is a negligible factor in the enzyme-substrate kinetics and is calculated to be less than 0.2 sec.-1. 4. The velocity constant, k3, for the enzymatic breakdown of peroxidase-H2O2 Complex I varies from nearly zero to higher than 5 sec.-1, depending upon the acceptor and its concentration. The quotient of k3 and the leucomalachite green concentration is 3.0 x 10(4) liter mole-1 sec.-1. For ascorbic acid this has a value of 1.8 x 10(5) liter mole-1 sec.-1. 5. For a particular acceptor concentration, k3 is determined solely from the enzyme-substrate kinetics and is found to be 4.2 sec.-1. 6. For the same conditions, k3 is determined from a simple relationship derived from mathematical solutions of the Michaelis theory and is found to be 5.2 sec.-1. 7. For the same conditions, k3 is determined from the over-all enzyme action and is found to be 5.1 sec.-1. 8. The Michaelis constant determined from kinetic data alone is found to be 0.44 x 10(-6). 9. The Michaelis constant determined from steady state measurements is found to be 0.41 x 10(-6). 10. The Michaelis constant determined from measurement of the overall enzyme reaction is f…

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