Suppose a reaction has
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Biochemistry: Concepts and Connections (2nd Edition)
- If the Gibbs free energy change for the reaction; Succinate + FAD →Fumarate + FADH2 is -40KJ/mol at 37° C. Calculate the ratio of FAD: FADH2 in this condition, if [Succinate]=0.75M and [Fumarate]=0.5M at this condition. Half reaction Standard reduction potential (in volts) Fumarate + 2H + 2 e →Succinate 0.031 FAD+2H+ + 2e →FADH2 -0.219arrow_forwardConsider the following reaction:ATP → AMP + 2 PiCalculate the equilibrium constant (Keq) given the following ΔG°′ values:ATP → AMP + PPi (−32.2 kJ/mol)PPi → 2Pi (−33.5 kJ/mol)arrow_forwardA certain first order reaction has the rate law Rate = k[A] with k=0.0068 sec-1. If the initial concentration of A is 0.75 M, what will be the concentration of A after 1 minute? What is the half-life for this reaction? How much time will it take for 75% of A to react? How much A will be left after the passage of three half-lives? What is the initial rate of the reaction?arrow_forward
- The decomposition of crystalline N2O5 N2O5(s) → 2NO2(g) + 1/2O2(g) is an example of a reaction that is thermodynamically favored, even though it absorbs heat. At 25 °C we have the following values for the standard state enthalpy and free energy changes of the reaction: ∆H° = +109.6 kJ/mol ∆G° = -30.5 kJ/mol (a) Calculate ∆S ° at 25 °C. (b) Why is the entropy change so favorable for this reaction?arrow_forwardAn enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min-1 when the substrate concentration is five times greater than the KM. What is the Vmax of this enzyme in µmol⋅min−1?arrow_forwardThe following data were obtained for a reaction that catalyzed by an enzyme: Initial concentration of 0.141 0.109 0.077 0.040 0.028 0.020 0.016 the enzyme [S], mol L- Relative velocity, V 22.0 20.5 19.0 12.5 9.0 7.0 6.0 For this reaction, the rate is found experimentally to follow the Michaelis-Menten equation: Vmax[S] Vo = Км+[S] (1) Transform the above equation into a straight-line equation. By plotting a suitable graph, determine the Michaelis constant (KM) and the maximal velocity (Vmax) for the above reaction. Determine the Vmax value when [S] = KM.arrow_forward
- For a Michaelis-Menten reaction, k₁=5 x 107/M-s, k-1-2 x 104/s, and k2=4 x 10²/s. Calculate the Ks and KM for this reaction. Does substrate binding achieve equilibrium or steady state?arrow_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_forwardCalculate ΔG°′ for the reaction A + B ⇌ C + D at 25°C when the equilibrium concentrations are [A] = 10 μM, [B] = 15 μM, [C] = 3 μM, and [D] = 5 μM. Is the reaction exergonic or endergonic under standard conditions?arrow_forward
- A simple biochemical reaction with three molecules has solutions that oscillate toward a steady state when positive constants a and b are below the curve b - a = (b + a)3. Find the largest possible value of a for which the reaction has solutions that oscillate toward a steady state. (Hint: Find where da/db = 0. Derive values for a + b and a - b, and then solve the equations in two unknowns.) Source: Mathematical Biology.arrow_forwardProduce a reading log for the sections in your text that discuss the Michaelis-Menten equation, including kat Focus on the derivation of the Michaelis-Menten equation. List and explain the assumptions underlying the Michalis-Menten equation. Provide definitions for each term. What is equal at equilibrium? What is the general expression Keg (the equilibrium constant) in terms of product and reactant concentra- tion?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_forward
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