E17C.1(b) The equilibrium constant for the binding of a drug molecule toa protein was measured as 200. In a separate experiment, the rate constantfor the binding process, which is second order overall, was found to be1.5 x 10 dm mol s. What is the rate constant for the first-orderdissociation of the drug molecule from the protein- drug complex?

Binding of substrate to active site of enzyme can be represented as

Answered: E17C.1(b) The equilibrium constant for…

Chemistry: The Molecular Science

5th Edition

ISBN:9781285199047

Author:John W. Moore, Conrad L. Stanitski

Publisher:John W. Moore, Conrad L. Stanitski

Chapter11: Chemical Kinetics: Rates Of Reactions

Section: Chapter Questions

Problem 83QRT

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For the reaction NH2SO2OH + H2O → NH4HSO4 In aqueous solution at 80.35oC, the following constants were observed at the indicated ionic strength μ x103 k (L/mol hr) 5.06 1.07 11.21 1.02 15.85 0.976 22.94 0.886 From these data ascertain: a.) the valence of the reacting ions and b.) the rate constant for the primary salt effect.
The frequency factor for a second-order gas-phase decomposition of a species at low pressures is 2.3 × 1013 dm3 mol−1 s−1 and its activation energy is 30.0 kJ mol−1. What are (i) the entropy of activation, (ii) the enthalpy of activation, (iii) the Gibbs energy of activation at 298 K? Assume κ = 1.
The enzyme-catalysed conversion of a substrate at 298 K has KM = 0.032 mol dm−3 and vmax = 4.25 × 10−4 mol dm−3 s−1 when the enzyme concentration is 3.60 × 10−9 mol dm−3. Calculate the catalytic efficiency of the enzyme, as defined in Exercise E17F.5(a).
) Calculate the activation energy for vacancy formation in aluminium, given that the equilibriumnumber of vacancies at 500°C (773 K) is 7.55 × 1023 m−3. The atomic weight and density (at500°C) for aluminium are, respectively, 26.98 g/mol and 2.62 g/cm3. (
Consider the reaction of [V(H2O)6]2+ with [Co(NH3)5X]2+ in acidic aqueous solution (X = halide or NCS–) producing [V(H2O)5X]2+ and [Co(H2O)6]2+. Suggest the mechanism, considering that the rate constant is very similar for X = Cl, Br, I. Characterize in few words individual steps. Explain the nature of the rate-determining step in terms of the [V(H2O)6]2+ electron configuration.
Provided the reaction A + 2B + C → 2D + E, and the set of data thatfollows:
Derive an expression for the time dependence of the degree of polymerization for the stepwise polymerization of a hydroxyacid HO−R−COOH for which the rate law is d[A]/dt = −kr[A]2[OH], where A denotes the carboxylic acid group.
The equilibrium constant for the binding of a drug molecule to a protein was measured as 200. In a separate experiment, the rate constant for the binding process, which is second order overall, was found to be 1.5 × 108 dm3 mol–1 s–1. What is the rate constant for the first-order dissociation of the drug molecule from the protein–drug complex?
The effective rate constant for a gaseous reaction which proceeds by a Lindemann–Hinshelwood mechanism is 1.7 × 10−3 s−1 at 1.09 kPa and 2.2 × 10−4 s−1 at 25 Pa. Calculate the rate constant for the activation step in the mechanism.
Calculate the magnitude of the diffusion-controlled rate constant at 320 K for the recombination of two atoms in water, for which η = 0.89 cP. Assuming the concentration of the reacting species is 1.5 mmol dm−3 initially, how long does it take for the concentration of the atoms to fall to half that value? Assume the reaction is elementary.
Discuss the assumptions made when deriving the Michaelis-Menten model of enzyme kinetics.
Calculate the ratio of rates of catalyzed to non-catalyzed reactions at 37°C, given that the Gibbs energy of activation for a particular reaction is reduced from 100 kJ/mol to 10 kJ/mol. Ans: 1.5 x 1015

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