Suppose a reaction has
Want to see the full answer?
Check out a sample textbook solutionChapter 3 Solutions
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_forwardIn the hydrolysis (saponification) of ethyl acetate, a plot of In(k,-k) against time is a straight line. The conductivity of the reaction mixture was 1438 μS cm after 10 min and 1030 μS cm after 40 min of mixing reaction components. If K∞ = 653 US cm, calculate the reaction rate constant in s. Select one: 1.1 × 10251 x 4.1 × 10-4 s1 8.1 x 10-5 51 2.5 × 10-3 s-1arrow_forwardThe 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_forward
- A 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_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_forwardThe standard reduction potentials for some important cellular compounds are shown below. Half-Reaction go' (V) O₂+ 2H + 2 e H₂O 0.815 Cytochrome a3 (Fe3+) + e¯ = cytochrome a3 (Fe2+) 0.385 Cytochrome a (Fe3+)+ e cytochrome a (Fe2+) 0.29 Cytochrome c (Fe3+)+ e cytochrome c (Fe2+) 0.235 Cytochrome c₁ (Fe3+) + e cytochrome c₁ (Fe2+) 0.22 Cytochrome b (Fe3+) + e cytochrome b (Fe2+) 0.077 Ubiquinone +2 H+ + 2e ubiquinol 0.045 Fumarate + 2H + 2 e succinate 0.031 FAD +2 H+ + 2e FADH2 (in flavoproteins) ~0. NAD+H+2 e NADH -0.315 NADP+ + H+ + 2 e¯ = NADPH -0.320 Based on this information, you can conclude that reduction is most favorable for NADH Oxygen Cytochrome C H+arrow_forwardsuppose the same experiment was done using the mixture of tube 2 of this experiment( as described in problem 1) in which Fe(SCN)2+ is assumed to form rather than FeSCN2+. That is, assume that equilibrium reaction 5 is the equilibrium that is occurring. Using the spectronic 20 the molarity of Fe(scn)2+ was found to be 0.265 x 10^04M. Write the chemical equilibrium equation ad the mathematical form of the equilibrium expression. calculate the initial molarity of Fe, HSCN, Fe(SCN)2+ and H. Calculate final molarity of Fe3+, HSCN, Fe(SCN)2+ and H+. What is the value of the equilibrium constant?arrow_forward
- Produce 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_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_forwardThe enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinatearrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON