QUESTION 2ADPAG"=-18.9 kJ/mol1,3-Bisphosphoglycerate → 3-PhosphoglycerateNormal free energy of the shown step of glycolysis coupled with synthesis of one molecule of ATP is -18.9 kJ/mol. Calculate AG" (in kJ/mol) of dephosphorylation of1,3-Biphosphoglycerate if AG"¹ of synthesis of ATP from ADP is 1.75.ATP AG" = 1.75 kJ/mol

Free energy change for biochemical reaction is given by ΔG°' = -R T ln Keq , where Keq is the…

Answered: QUESTION 2 ADP ATP AG"= 1.75 kJ/mol…

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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QUESTION 37 Key enzymes in glycolysis and the Krebs cycle are allosterically regulated. Which of the following is FALSE? O a. The main control point of glycolysis is the enzyme phosphofructokinase. Ob. The main control point in the citric acid cycle is isocitrate dehydrogenase Oc. Isocitrate dehydrogenase is inhibited by ATP or NADH. O d. Phosphofructokinase is activated by citrate and ATP. Oe. If ATP levels are high and the citric acid cycle shuts down, acetyl CoA is diverted to the synthesis of fatty acids for storage lick Save and Submit to save and submit. Click Save All Answers to save all answers. S # 20 F3 $ F4 % L5 MacBook Pro
QUESTION 31 Four competitive inhibitors of an enzyme were found to exhibit the following K¡ values. Which is the worst inhibitor? K = 7x 10-5 M K1 = 3 x 10-6 M KI = 1 x 10-4 M K1 = 6 x 10-8 M QUESTION 32 What is the Km for a Michaelis enzyme if the 1/concentration of substrate intercept is -5.73e Mon a Lineweaver Burk plot of its reaction kinetics? Give your answer in 3 sigfīgs in scientific notation, for example, 1.52 e QUESTION 33 What is the charge of an ionized peptide in the mass spectrometer if its isotopic peaks are 0.20 m/z apart? O 6+ O 5+ wers to save all answers. stly cloud
Question 1 a. What enzyme works on glucose-6-P when the energy charge is 0.80? b. What enzyme works on glucose-6-P when the energy charge is 0.97? c. What enzyme works on glycogen when the energy charge is 0.80?d. d. What enzyme works on glycogen when the energy charge is 0.97? e. What enzyme works on pyruvate when the energy charge is 0.80 (assume high O2)? f. What enzyme works on pyruvate when the energy charge is 0.97?
QUESTION 18 Explain the reason why at low ATP concentrations the velocity of PFK-1 is faster than when high ATP concentrations are present. Low (ATP) High (ATP) (Fructose 6-phosphate) PFK-1 activity
Question #3 Complex III (cytochrome bc₁ complex) in the electron transport chain transfers electrons from reduced coenzyme Q to cytochrome c. 3A. Write a balanced equation for the overall redox reaction performed by complex III. Indicate the electron donor and acceptor in the redox reaction. [Do not include the intermediates in this overall reaction. Do not account for proton pumping]. 3B. Calculate the change in the standard reduction potential for this reaction. [see table on page 2]. 3C Which has a lower amount of free energy at the standard state, the products or the reactants?
Question #2: Consider the following data for Cell G run in 1 L chemostat, with a feed containing 30 g/L substrate: Feedrate (ml/hr) (c) Calculate 27.5 24.2 22.1 18.8 Steady State Cell Mass Concentration (g/L) 12.0 14.7 15.8 16.7 Steady State Substrate Concentration (g/L) 10.0 5.56 (d) Using the calculated kinetic parameters, 3.70 (a) Determine the kinetic parameters for growth (b) At each dilution rate, calculate Yx/s. Is it constant with dilution rate and substrate concentration? 2.23 (i) the critical dilution rate, D. (ii) the dilution rate corresponding to maximum productivity, Dm (iii) the maximum cell productivity (cells/L/hr) (i) Generate a plot of X and S vs D for a feed concentration of 25 g/L. (ii) What is the critical dilution rate for this condition? (iii) What is the dilution rate corresponding to maximum productivity at this condition? (iv) What is the maximum cell productivity at this condition? (v) For a reactor operating at this maximum productivity, what would be the…
QUESTION 1 Using the free energy values of glycolysis and pyruvate transformation to ethanol calculate free energy (in kJ/mol) of glucose fermentation to ethanol: Glucose + 2 ADP + 2 Pi ⇌ 2 Ethanol + 2CO2 + 2 ATP + 2 H2O
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Question 3: A runner just finished a marathon. For the enzymes listed below, indicate whether the enzyme activity is upregulated (1) or downregulated (↓) in the muscle and liver, respectively. Enzyme (a) Glycogen synthase (b) Phosphofructokinase-1 (c) Fructose-Bisphosphatase-2 (d) Pyruvate kinase (e) Pyruvate carboxylase (f) Acetyl-CoA carboxylase Muscle Liver
Question 2 The Michaelis Menten equation for enzyme kinetics can accurately predict when a single enzyme will catalyze one substrate molecule into product. True O False
Question 1: The amount of energy effectively stored in each ATP (the actual energy of ATP hydolysis) will depend on the concentrations of ATP, ADP, and Pi, according to equations discussed in class and in the book. If the ATP synthase is operating at close to equilibrium (as might be the case if ATP is being used slowly), we can compute the maximum possible energy of ATP hydrolysis by assuming balance between the energy provided by the proton gradient and the energy used to make the ATP. (Since we care about the magnitude of the energy it’s convenient to talk in terms of absolute values; the maximum possible ATP hydrolysis energy is then the most negative value possible.) Using what you know about the mechanism of the ATP synthase, and assuming that the membrane gradient consists of a Δψ of -.15V and a ΔpH of 1 unit (alkaline inside), compute the maximum possible ATP-hydrolysis energies for synthases with: a.) 8 c-subunits b.) 13 c-subunits
Question 1: The standard reduction potential for the the cytochrome c Fe3+/Fe2+ redox couple and for the dioxygen/water redox couple. Part a: Use these values, and the relevant equation, to compute the standard free energy change for the transfer of 4 electrons from cytochrome c to dioxygen. Part b: Next, compute the free energy needed to pump four protons across the mitochondrial membrane, using the relevant equation and values of -.14V for Δψ and 1.4 for ΔpH. Part c: If energy conservation by cytochrome c oxidase involved only the four pumped protons (and standard conditions applied), what would be the efficiency of energy conservation at this step? (what is the ratio [energy conserved in the gradient] / [redox energy used] ?)

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