5. Select the rate law for ES formation dES/dt A. kcatlES 5. Select the rate law for ES formation dES/dt A. kcatlES
Km represents the.... formation of EP the back reaction of product to ES formation of ES kcat Km represents the.... formation of EP the back reaction of product to ES formation of ES kcat
2. In a single substrate enzyme-catalyzed reaction, the forward rate constant (formation of ES) is 2.1x105 M-1 s-1 , the reverse rate constant (dissociation of ES to E +S) is 9.4x103 s-1 , and the catalytic rate constant (turnover of ES to P) is 7.2x102 s-1 . From this data, KM is:
2. Consider the nonlinear autonomous system of DEs: dx dt dy dt (a) Find all critical points of this system. (Make sure that you have found all of them.) (b) Find the linearization (a linear system) at each critical point. Calculate the eigen- values of the contant coefficient matrix, classify the corresponding critical point, and state its stability.
N205 - NO3 + NO2 the observed rate law is rate = k[N205). If-dN205/dt = 0.20 M/min when [N205) = 0.12 M, what is the value of the rate constant? O a. 0.32 min1 O 6.0.60 min-1 OC. 0.024 min-1 O d. none of these Oe. 1.7 min-1
6. Use the steady state approximation to derive a rate law for d[D/dt with the following mechanism A+B +C Step 1) Step 2) 7. a) What is the rate law for the mechanism in question (6) if the second step is the rate-limiting step? b) Express the activation energy for the overall reaction in terms of the activation energies for each step in the mechanism from part (a)
The rate law for the decomposition of PH3 is, R = -d[PH3]/dt = k[PH3]. It takes 120 s for the concentration of 0.84 M PH3 to decrease to 0.21 M. How much time is required for 1.5 M PH3 to decrease to 0.56 M?
The rate law for the decomposition of PH3 is, R = -d[PH3]/dt = k[PH3]. It takes 120 s for the concentration of 0.84 M PH3 to decrease to 0.21 M. How much time is required for 1.5 M PH3 to decrease to 0.56 M?
dt Newton's law of cooling states that the rate of change in the temperature (t) of a body is proportional to the difference between the temperature of the medium M(t) and the dT temperature of the body. That is, = K[M(1) – TCC), where is a constant. Let K = 0.03 (min) and the temperature of the medium be constant, m(t) = 295 kelvins. If the body is initially at 364 kelvins, use Euler's method with h = 0.1 min...
± Experimental Determination of a Rate Law Part B: Calculate the initial rate for the formation of C at 25 ∘C, if [A]=0.50M and [B]=0.075M. Express your answer to two significant figures and include the appropriate units. Consider the reaction A+2B⇌C whose rate at 25 ∘C was measured using three different sets of initial concentrations as listed in the following table: Trial [A] (M) [B] (M) Rate (M/s) 1 0.50 0.030 9.0×10−3 2 0.50 0.060 1.8×10−2 3 1.00 0.030 3.6×10−2
Enzyme E bind to substrate S to form ES complex leading to product formation. However, the ES complex also undergoes suicidal inactivation that would result in the loss of the total enzyme activity. In addition, after the binding of S to E there exposes another binding site in E for uncompetitive inhibitor I. The ESI complex does not have the capacity to form product and would not undergo inactivation. The equilibriums, reactions and the kinetic parameters involved can be represented...