Suppose that, in the absence of a catalyst, a certain biochemical reaction occurs x times per second at normal body temperature 137 °C2. In order to be physiologically useful, the reaction needs to occur 5000 times faster than when it is uncatalyzed. By how many kJ>mol must an enzyme lower the activation energy of the reaction to make it useful?

For the reaction, 2NO(g) + Cl2(g) 2NOCI(g), the following data were obtained at constant temperature: [NO] Initial rate Experiment (M) (M) (M/s) 1 0.20 0.10 0.63 2 0.20 0.30 5.67 3 0.80 0.10 2.52 4 0.30 0.20 What is the initial rate of reaction for Experiment 4? 5.7 M/s 1.9 M/s 6.7 M2s1 3.8 M/s 2.8 M/s

The activation barrier for the hydrolysis of sucrose into glucose and fructose is 108 kJ>mol. If an enzyme increases the rate of the hydrolysis reaction by a factor of 1 million, how much lower must the activation barrier be when sucrose is in the active site of the enzyme? (Assume that the frequency factors for the catalyzed and muncatalyzed reactions are identical and a temperature of 25 °C.)

A certain 2nd order reaction is known to proceed by a two-step process such that k1<<k2.  The forward reaction has an activation energy of 48 kJ/mole and the reverse reaction has an activation energy of 62 kJ/mole.  Sketch the energy diagram for the reaction.