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The initial rates at various substrate concentrations for an enzyme-catalyzed reaction are as follows:
[S], M vo, M/min2.50 x 10-5 3.80 x 10-54.00 x 10-5 5.34 x 10-56.00 x 10-5 6.86 x 10-58.00 x 10-5 8.00 x 10-51.60 x 10-4 1.068 x 10-42.00 x 10-4 1.140 x 10-4
a) Does this reaction follow Michaelis-Menten kinetics?
b) Calculate the values of vmax and Km for the reaction.
c) How much of a noncompetitive inhibitor must be added to yield 90% inhibition? The degree of inhibition, i, is calculated by i% = (1-?) 100%, where ? = (vo)inhibition/ vo Assume KI = 2.9 x 10-4 M.
Show all the steps in the mechanism for the following reaction, When benzene is mixed with deuterated sulfuric acid, deuterium is slowly incorporated onto the ring. Show the mechanism for this reaction and explain how this relates the sulfonation of ..
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