If the Gibbs free energy change for the reaction; Succinate + FAD →Fumarate + FADH2is -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 reactionStandard reduction potential (in volts)Fumarate + 2H + 2 e →Succinate0.031FAD+2H+ + 2e →FADH2-0.219

Biological oxidation-reduction reactions involve the transfer of electrons from one biomolecule,…

Answered: If the Gibbs free energy change for the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The kinetic data of an enzymatic reaction shown in the following table: a. Calculate the Km and Vmax of the reactionb. A competitive inhibitor is added to the reaction at a concentration of 5 μM, determine the new Vmax of the reaction and what happened to the Km value.
Consider the following reaction and its equilibrium constant: 12(g) 21(g) Kp = 0.209 atm A reaction mixture contains 0.89 atm 12 and 1.77 atm I. Which of the following statements is TRUE concerning this system?
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
Calculate AG for this reaction under the following conditions: 37°C, pH 7, [Pyruvate] = [CO₂] = 4.0 mM, [OAA] = 2.0 mM, [ATP] = 3.5 mM, [P;] = 5.0 mM, and [ADP] = 1.8 mM. Use 2 signficant figures. AG= i kJ.mol-1 Under these conditions, the reaction is (Tolerance is +/- 2%)
Consider the following reaction at 25°C with the ΔG°’ = +1800 J/mol for the forward reaction.The molar concentrations at the beginning of the reaction were [A] = 19 mM and [B] = 10 mM.After 1 hour, the concentrations were [A] = 16 mM and [B] = 13 mM. Calculate the ΔG of the reaction at the 1 hour timepoint. Please round to 1 decimal point.Gas constant = 8.315 J/mol K
Calculate the Gibbs free energy change (G) for the following chemical reaction: glutamate + NH3 glutamine + H2OThe reaction occurs at 293 K, the change in heat (H) = 4103 cal, and the change in entropy (S) = 2.4 cal/K.
A particular reaction has a ΔG‡ of 30.0 kJ mol-1 at 25.0 °C. In the presence of an enzyme, the same reaction has a ΔG‡ of 1.50 kJ mol-1 at the same temperature. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.
For an enzyme following Michaelis-Menten kinetics, the following Vo vs. S data were obtained in steady state experiments using 2 micromolar enzyme for all measurements: [S] Vo 1 mM 4.0 mM/min 2 mM 4.8 mM/min 4 mM 4.9 mm/min 8 mM 4.95 mM/min Estimate the value of kcat for the reaction. Be sure to include the appropriate units.
Calculate theequilibrium constant and thefree energy of (Mg)ATP hydrolysis in a closed system in which concentrations of ATP, ADP and Piare, respectively, 3.5, 1.0, and 5 mMand 25 degrees Celsius. Is the reaction spontaneous?R = 8.314 J/(deg Kelvin-mol).
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?
The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Vo (micromol/min) Substrate added (mM) 200 1.0 400 2.0 800 4.0 1600 8.0 3200 16.0 The enzyme concentration used in all reactions is 106 M. Which of the following is true: O A) The Km for the reaction must be less than 1 mM ○ B) It is possible to determine Km for the reaction, but not Vmax or kcat OC) It is possible to determine only kcat, not Vmax or Km D) It is not possible to determine Vmax for the reaction OE) The ratio Vmax/Km for the reaction cannot be determined

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