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Consider the simple bimolecular reaction
Since the law of mass action governs reaction kinetics, the forward and reverse fluxes, J, can be defined as:
ΔG can be defined in terms of the ratio of forward and reverse fluxes:
Derive this equation.
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Chapter 11 Solutions
Pearson eText for Biochemistry: Concepts and Connections -- Instant Access (Pearson+)
- A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.arrow_forwardAn enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :arrow_forwardA bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 m mol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM?arrow_forward
- discuss the following statement: “Whether the ΔG for a reaction is larger, smaller, or the same as ΔG° depends on the concentration of the compounds that participate in the reaction.”arrow_forwardThe following questions are based on the reaction A+ B ↔ C+D shown in Figure 8.1. 1. Which of the following terms best describes the progress of the reaction with respect to free energy change? a) endergonic, ∆G> 0 b) exergonic, ∆G> 0 c) exergonic, ∆G< 0 d) endergonic, ∆G< 0 2. Which of the following in Figure 8.1 remains unchanged by having an enzyme included? a) b b) d c) a d) c 3. The part labeled “C” on the above graph represents a) Energy of activation without enzyme b) Energy of activation with enzyme c) Amount of free energy released d) amount of energy required for the reaction progressarrow_forwardThe equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)arrow_forward
- All of the following statements are true about the relationships between [S], Km and Vmax EXCEPT: а. As the [S] is increased, v approaches the limiting value, Vmax. b. Km= Vmax/2. The rate of the reaction, v, follows a first order rate equation v = K'[A] and K'= Vmax/Km. The rate of product formed, v, is at Vmax when [S] >> Km. с. d.arrow_forwardFor the following reaction X + YA + B at 300 K, it is found equilibrium constant equal to 10. Therefore, AG & AGⓇ of the reaction at 300 K respectively are - Answer barrow_forwardDerive an Equation that explains the realtionship between kE and kN with respect to the equilibrium constants provided in the reaction scheme provided below. Assume that the enzyme must bind with A before it binds with B. The two reactions are related by the following reaction scheme:provided below.arrow_forward
- The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"arrow_forwardCalculate the standard free energy change (ΔG°′) for the following reaction: ½ O2 + FADH2 → H2O + FADarrow_forwardThe Michaelis-Menten equation for the enzyme chymotrypsin is 0.14[S] v : 0.015 + [S] where v is the rate of an enzymatic reaction and [S] is the concentration of a substrate S. Calculate dv/d[S] and interpret it.arrow_forward
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